Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

F0KMG6 (F0KMG6_ACICP) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme By similarity. HAMAP-Rule MF_01646 SAAS SAAS019478

Catalytic activity

Precorrin-2 + NAD+ = sirohydrochlorin + NADH. HAMAP-Rule MF_01646 SAAS SAAS019478

S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2. HAMAP-Rule MF_01646 SAAS SAAS019478

S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1. HAMAP-Rule MF_01646 SAAS SAAS019478

Siroheme + 2 H+ = sirohydrochlorin + Fe2+. HAMAP-Rule MF_01646 SAAS SAAS019478

Pathway

Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. HAMAP-Rule MF_01646 SAAS SAAS019478

Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. HAMAP-Rule MF_01646 SAAS SAAS019478

Porphyrin-containing compound metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. HAMAP-Rule MF_01646 SAAS SAAS019478

Porphyrin-containing compound metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1. HAMAP-Rule MF_01646 SAAS SAAS019478

Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. HAMAP-Rule MF_01646 SAAS SAAS019478

Sequence similarities

Belongs to the precorrin methyltransferase family. RuleBase RU003960

In the C-terminal section; belongs to the precorrin methyltransferase family. HAMAP-Rule MF_01646

In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family. HAMAP-Rule MF_01646

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding22 – 232NAD By similarity HAMAP-Rule MF_01646
Nucleotide binding43 – 442NAD By similarity HAMAP-Rule MF_01646
Region1 – 204204precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase By similarity HAMAP-Rule MF_01646
Region216 – 457242Uroporphyrinogen-III C-methyltransferase By similarity HAMAP-Rule MF_01646
Region301 – 3033S-adenosyl-L-methionine binding By similarity HAMAP-Rule MF_01646
Region331 – 3322S-adenosyl-L-methionine binding By similarity HAMAP-Rule MF_01646

Sites

Active site2481Proton acceptor By similarity HAMAP-Rule MF_01646
Active site2701Proton donor By similarity HAMAP-Rule MF_01646
Binding site2251S-adenosyl-L-methionine; via carbonyl oxygen By similarity HAMAP-Rule MF_01646
Binding site3061S-adenosyl-L-methionine; via carbonyl oxygen By similarity HAMAP-Rule MF_01646
Binding site3831S-adenosyl-L-methionine; via amide nitrogen By similarity HAMAP-Rule MF_01646
Binding site4121S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity HAMAP-Rule MF_01646

Amino acid modifications

Modified residue1291Phosphoserine By similarity HAMAP-Rule MF_01646

Sequences

Sequence LengthMass (Da)Tools
F0KMG6 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: BA82A6BACB08FC81

FASTA45750,291
        10         20         30         40         50         60 
MDIFPISLKL QQQYCLIVGG GHIALRKANL LAKAGAVIDI IAPAIEEQLL QLVKTTGGEY 

        70         80         90        100        110        120 
FAESFAEKIL NTPYRLVIAA TNDAQVNKAV FEQCEARNLL VNSVDDIPHC RFMVPAIIDR 

       130        140        150        160        170        180 
SPLIISVASN GASPVLSRQL RTQIETIVPH GMGKLAEFSG QWRKQVKEKI PNPDERRIFW 

       190        200        210        220        230        240 
ENLYASPLKE QVFNDNLEVA NGLIQQALTE WTAPKGEVYL VGAGPGDPEL LTLKALRLMQ 

       250        260        270        280        290        300 
QADVVIYDRL VSAPILELCR RDATKIYVGK ARSNHSVPQD GINALLVEYA QKGKRVCRLK 

       310        320        330        340        350        360 
GGDPFIFGRG GEEIQELVEA NVTFQVVPGI TAASGCSAYA GIPLTHRDYA QSVRFLTGHL 

       370        380        390        400        410        420 
KEGSPELPWN ELVYENQTLV LYMGLVGLER ICEQLIAHGQ RADMPVALIS KGTTPDQKVV 

       430        440        450 
VGTLADIATK VSEHHIVAPT LTIIGEVVNL REQLKWQ 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of a nonpathogenic wastewater-adapted bacterium Acinetobacter calcoaceticus PHEA-2 and comparative genomics insights into environmental adaptation."
Zhan Y., Yan Y., Zhang W., Chen M., Ping S., Lu W., Lin M.
Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: PHEA-2.
[2]"Genome sequence of Acinetobacter calcoaceticus PHEA-2, isolated from industry wastewater."
Zhan Y., Yan Y., Zhang W., Yu H., Chen M., Lu W., Ping S., Peng Z., Yuan M., Zhou Z., Elmerich C., Lin M.
J. Bacteriol. 193:2672-2673(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PHEA-2 EMBL ADY82761.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002177 Genomic DNA. Translation: ADY82761.1.
RefSeqYP_004996443.1. NC_016603.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADY82761; ADY82761; BDGL_002175.
GeneID11636698.
KEGGacc:BDGL_002175.
PATRIC47082490. VBIAciCal168233_2176.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK02302.
OMAQASFIMP.

Enzyme and pathway databases

BioCycACAL871585:GH86-2203-MONOMER.
UniPathwayUPA00148; UER00211.
UPA00148; UER00222.
UPA00262; UER00211.
UPA00262; UER00222.
UPA00262; UER00376.

Family and domain databases

Gene3D1.10.8.210. 1 hit.
3.30.950.10. 1 hit.
3.40.1010.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPMF_01646. Siroheme_synth.
InterProIPR000878. 4pyrrol_Mease.
IPR014777. 4pyrrole_Mease_sub1.
IPR014776. 4pyrrole_Mease_sub2.
IPR006366. CobA/CysG_C.
IPR016040. NAD(P)-bd_dom.
IPR012409. Sirohaem_synth.
IPR019478. Sirohaem_synthase_dimer_dom.
IPR006367. Sirohaem_synthase_N.
IPR003043. Uropor_MeTrfase_CS.
[Graphical view]
PfamPF10414. CysG_dimeriser. 1 hit.
PF13241. NAD_binding_7. 1 hit.
PF00590. TP_methylase. 1 hit.
[Graphical view]
PIRSFPIRSF036426. Sirohaem_synth. 1 hit.
SUPFAMSSF53790. SSF53790. 1 hit.
TIGRFAMsTIGR01469. cobA_cysG_Cterm. 1 hit.
TIGR01470. cysG_Nterm. 1 hit.
PROSITEPS00839. SUMT_1. 1 hit.
PS00840. SUMT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF0KMG6_ACICP
AccessionPrimary (citable) accession number: F0KMG6
Entry history
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: July 9, 2014
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)