hemC:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

HemC

Synonyms

hydroxymethylbilane synthase[1], B3805[2][1], PopE[2][1], HemC[2][1] , ECK3799, JW5932, popE, b3805

Product description

Porphobilinogen deaminase; neomycin sensitivity[3]

EC number (for enzymes)
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Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0005737

cytoplasm

C

Seeded from Riley et al 2006 [1].

Missing: evidence, reference

GO:0004418

hydroxymethylbilane synthase activity

PMID:379277[4]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0004418

hydroxymethylbilane synthase activity

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00260

F

Seeded from EcoCyc (v14.0)

complete

GO:0006783

heme biosynthetic process

PMID:379277[4]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0004418

hydroxymethylbilane synthase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000860

F

Seeded from EcoCyc (v14.0)

complete

GO:0033014

tetrapyrrole biosynthetic process

PMID:379277[4]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0004418

hydroxymethylbilane synthase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:2.5.1.61

F

Seeded from EcoCyc (v14.0)

complete

GO:0018160

peptidyl-pyrromethane cofactor linkage

PMID:8727319[5]

IDA: Inferred from Direct Assay

P

complete

GO:0006779

porphyrin biosynthetic process

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00260

P

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

PMID:3052434[6]

IDA: Inferred from Direct Assay

C

complete

GO:0006779

porphyrin biosynthetic process

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0627

P

Seeded from EcoCyc (v14.0)

complete

GO:0033035

dipyrromethane cofactor binding

PMID:8727319[5]

IDA: Inferred from Direct Assay

1

Seeded from EcoCyc (v14.0)

complete

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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence
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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes
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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc 

MLDNVLRIAT RQSPLALWQA HYVKDKLMAS HPGLVVELVP MVTRGDVILD TPLAKVGGKG
LFVKELEVAL LENRADIAVH SMKDVPVEFP QGLGLVTICE REDPRDAFVS NNYDSLDALP
AGSIVGTSSL RRQCQLAERR PDLIIRSLRG NVGTRLSKLD NGEYDAIILA VAGLKRLGLE
SRIRAALPPE ISLPAVGQGA VGIECRLDDS RTRELLAALN HHETALRVTA ERAMNTRLEG
GCQVPIGSYA ELIDGEIWLR ALVGAPDGSQ IIRGERRGAP QDAEQMGISL AEELLNNGAR
EILAEVYNGD APA
Length

313

Mol. Wt

33.852 kDa

pI

4.4 (calculated)

Extinction coefficient

18,450 - 18,950 (calc based on 5 Y, 2 W, and 4 C residues)

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Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Domain

5..217

PF01379 Porphobilinogen deaminase, dipyromethane cofactor binding domain

PMID:19920124[7]

Domain

225..298

PF03900 Porphobilinogen deaminase, C-terminal domain

PMID:19920124[7]

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Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=hemC taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:49176416

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:947759

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0012427

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P06983

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10429

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10429

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:947759

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000422

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0424

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  4. ↑ 4.0 4.1 4.2 McConville, ML & Charles, HP (1979) Mutants of Escherichia coli K12 accumulating porphobilinogen: a new locus, hemC. J. Gen. Microbiol. 111 193-200 PubMed
  5. ↑ 5.0 5.1 Louie, GV et al. (1996) The three-dimensional structure of Escherichia coli porphobilinogen deaminase at 1.76-A resolution. Proteins 25 48-78 PubMed
  6. ↑ Jordan, PM et al. (1988) Purification, crystallization and properties of porphobilinogen deaminase from a recombinant strain of Escherichia coli K12. Biochem. J. 254 427-35 PubMed
  7. ↑ 7.0 7.1 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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