AHBA_METBF
ID AHBA_METBF Reviewed; 182 AA.
AC Q46CH6;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Siroheme decarboxylase alpha subunit {ECO:0000305};
DE EC=4.1.1.111 {ECO:0000269|PubMed:24669201, ECO:0000269|PubMed:24865947};
DE AltName: Full=SH decarboxylase AhbAB {ECO:0000303|PubMed:24669201};
GN Name=ahbA {ECO:0000303|PubMed:24669201};
GN OrderedLocusNames=Mbar_A1459 {ECO:0000312|EMBL:AAZ70416.1};
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, AND SUBUNIT.
RX PubMed=24669201; DOI=10.1155/2014/327637;
RA Kuehner M., Haufschildt K., Neumann A., Storbeck S., Streif J., Layer G.;
RT "The alternative route to heme in the methanogenic archaeon Methanosarcina
RT barkeri.";
RL Archaea 2014:327637-327637(2014).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, AND SUBUNIT.
RX PubMed=24865947; DOI=10.1111/mmi.12656;
RA Palmer D.J., Schroeder S., Lawrence A.D., Deery E., Lobo S.A.,
RA Saraiva L.M., McLean K.J., Munro A.W., Ferguson S.J., Pickersgill R.W.,
RA Brown D.G., Warren M.J.;
RT "The structure, function and properties of sirohaem decarboxylase--an
RT enzyme with structural homology to a transcription factor family that is
RT part of the alternative haem biosynthesis pathway.";
RL Mol. Microbiol. 93:247-261(2014).
CC -!- FUNCTION: Involved in siroheme-dependent heme b biosynthesis. Catalyzes
CC the decarboxylation of siroheme into didecarboxysiroheme.
CC {ECO:0000269|PubMed:24669201, ECO:0000269|PubMed:24865947}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + siroheme = 12,18-didecarboxysiroheme + 2 CO2;
CC Xref=Rhea:RHEA:19093, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:60052, ChEBI:CHEBI:140497; EC=4.1.1.111;
CC Evidence={ECO:0000269|PubMed:24669201, ECO:0000269|PubMed:24865947};
CC -!- ACTIVITY REGULATION: Binds heme b (PubMed:24669201, PubMed:24865947).
CC The redox state of the heme b modulates the activity of the enzyme
CC (PubMed:24865947). Activity is stimulated by sodium dithionite
CC (PubMed:24865947). {ECO:0000269|PubMed:24669201,
CC ECO:0000269|PubMed:24865947}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000269|PubMed:24669201,
CC ECO:0000269|PubMed:24865947}.
CC -!- SUBUNIT: Forms an heterodimer composed of AhbA and AhbB.
CC {ECO:0000269|PubMed:24669201, ECO:0000269|PubMed:24865947}.
CC -!- SIMILARITY: Belongs to the Ahb/Nir family. {ECO:0000305}.
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DR EMBL; CP000099; AAZ70416.1; -; Genomic_DNA.
DR AlphaFoldDB; Q46CH6; -.
DR SMR; Q46CH6; -.
DR STRING; 269797.Mbar_A1459; -.
DR EnsemblBacteria; AAZ70416; AAZ70416; Mbar_A1459.
DR KEGG; mba:Mbar_A1459; -.
DR eggNOG; arCOG01629; Archaea.
DR HOGENOM; CLU_112007_1_0_2; -.
DR OMA; EVSHNYL; -.
DR BRENDA; 4.1.1.111; 3250.
DR UniPathway; UPA00252; -.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000485; AsnC-type_HTH_dom.
DR InterPro; IPR040523; AsnC_trans_reg2.
DR InterPro; IPR019888; Tscrpt_reg_AsnC-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF17805; AsnC_trans_reg2; 1.
DR Pfam; PF13404; HTH_AsnC-type; 1.
DR SMART; SM00344; HTH_ASNC; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW Heme biosynthesis; Lyase.
FT CHAIN 1..182
FT /note="Siroheme decarboxylase alpha subunit"
FT /id="PRO_0000450505"
SQ SEQUENCE 182 AA; 20904 MW; D3E6423878739293 CRC64;
MIDIDNLKDQ LKKEAADFSC DMDTNDREVP VIELDETDKK ILNLIQQEVP LEVEPFAKLG
EILGLSETEV IERLRELNRK GAVRRVGPVL SMRNMGGVST LVALKVPESR IEEVAIFINE
YPEVSHNYLR SASQYNLWFT LSAPNKNRLE RILSEIREKT GCPLLDLPTK HLFKIQVKFD
IR
