ID   AHBA_OLEA2              Reviewed;         164 AA.
AC   Q30Y72;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Siroheme decarboxylase alpha subunit {ECO:0000305};
DE            EC=4.1.1.111 {ECO:0000269|PubMed:21969545};
GN   Name=ahbA {ECO:0000303|PubMed:21969545};
GN   OrderedLocusNames=Dde_2578 {ECO:0000312|EMBL:ABB39374.1};
OS   Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
OS   (Desulfovibrio alaskensis).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Oleidesulfovibrio.
OX   NCBI_TaxID=207559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
RX   PubMed=21685289; DOI=10.1128/jb.05400-11;
RA   Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA   Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R.,
RA   Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S.,
RA   Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT   "Complete genome sequence and updated annotation of Desulfovibrio
RT   alaskensis G20.";
RL   J. Bacteriol. 193:4268-4269(2011).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBUNIT.
RC   STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
RX   PubMed=21969545; DOI=10.1073/pnas.1108228108;
RA   Bali S., Lawrence A.D., Lobo S.A., Saraiva L.M., Golding B.T., Palmer D.J.,
RA   Howard M.J., Ferguson S.J., Warren M.J.;
RT   "Molecular hijacking of siroheme for the synthesis of heme and d1 heme.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:18260-18265(2011).
CC   -!- FUNCTION: Involved in siroheme-dependent heme b biosynthesis. Catalyzes
CC       the decarboxylation of siroheme into didecarboxysiroheme.
CC       {ECO:0000269|PubMed:21969545}.
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:21969545};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC       biosynthesis. {ECO:0000269|PubMed:21969545}.
CC   -!- SUBUNIT: Forms an heterodimer composed of AhbA and AhbB.
CC       {ECO:0000269|PubMed:21969545}.
CC   -!- SIMILARITY: Belongs to the Ahb/Nir family. {ECO:0000305}.
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DR   EMBL; CP000112; ABB39374.1; -; Genomic_DNA.
DR   RefSeq; WP_011368422.1; NC_007519.1.
DR   AlphaFoldDB; Q30Y72; -.
DR   SMR; Q30Y72; -.
DR   STRING; 207559.Dde_2578; -.
DR   EnsemblBacteria; ABB39374; ABB39374; Dde_2578.
DR   KEGG; dde:Dde_2578; -.
DR   eggNOG; COG1522; Bacteria.
DR   HOGENOM; CLU_112007_1_0_7; -.
DR   OMA; NVWFTFI; -.
DR   OrthoDB; 1844486at2; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000002710; Chromosome.
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; Reference proteome.
FT   CHAIN           1..164
FT                   /note="Siroheme decarboxylase alpha subunit"
FT                   /id="PRO_0000450502"
SQ   SEQUENCE   164 AA;  18482 MW;  3E659FD0FAD8C313 CRC64;
     MTGPAVQDQE LDQFDKKILD IIQTGFPLEP RPYAVIGDAV GLTEAEALAR VRALKERKII
     RRLGANFNSW KLGFRSTLCA AKVPEDKFDE FVAEVNSHVG VTHNYLRAHA YNVWFTFIGP
     SWEEVCSTLD SITQKTGIPI LNLPAEELYK IRVDFKMDED PAAD