ID   AHBD_OLEA2              Reviewed;         388 AA.
AC   Q30Y73;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=AdoMet-dependent heme synthase {ECO:0000305};
DE            EC=1.3.98.6 {ECO:0000269|PubMed:21969545};
GN   Name=ahbD {ECO:0000303|PubMed:21969545};
GN   OrderedLocusNames=Dde_2577 {ECO:0000312|EMBL:ABB39373.2};
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, COFACTOR, AND PATHWAY.
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 conversion of Fe-coproporphyrin III into heme by the oxidative
CC       decarboxylation of two propionate side chains.
CC       {ECO:0000269|PubMed:21969545}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Fe-coproporphyrin III + 2 S-adenosyl-L-methionine = 2 5'-
CC         deoxyadenosine + 2 CO2 + heme b + 2 L-methionine;
CC         Xref=Rhea:RHEA:56520, ChEBI:CHEBI:16526, ChEBI:CHEBI:17319,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:60344,
CC         ChEBI:CHEBI:68438; EC=1.3.98.6;
CC         Evidence={ECO:0000269|PubMed:21969545};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000269|PubMed:21969545};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC       biosynthesis. {ECO:0000269|PubMed:21969545}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. {ECO:0000305}.
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DR   EMBL; CP000112; ABB39373.2; -; Genomic_DNA.
DR   RefSeq; WP_011368421.1; NC_007519.1.
DR   AlphaFoldDB; Q30Y73; -.
DR   SMR; Q30Y73; -.
DR   STRING; 207559.Dde_2577; -.
DR   EnsemblBacteria; ABB39373; ABB39373; Dde_2577.
DR   KEGG; dde:Dde_2577; -.
DR   eggNOG; COG0535; Bacteria.
DR   HOGENOM; CLU_009273_4_0_7; -.
DR   OrthoDB; 1172757at2; -.
DR   UniPathway; UPA00252; -.
DR   Proteomes; UP000002710; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR034391; Cmo-like_SPASM_containing.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR017200; PqqE-like.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR030896; rSAM_AhbD_hemeb.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF13186; SPASM; 1.
DR   PIRSF; PIRSF037420; PQQ_syn_pqqE; 1.
DR   SFLD; SFLDF00542; alternative_heme_biosynthesis; 1.
DR   SFLD; SFLDG01387; BtrN-like_SPASM_domain_contain; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR04545; rSAM_ahbD_hemeb; 1.
DR   TIGRFAMs; TIGR04085; rSAM_more_4Fe4S; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Heme biosynthesis; Iron; Iron-sulfur; Metal-binding;
KW   Oxidoreductase; Reference proteome; S-adenosyl-L-methionine.
FT   CHAIN           1..388
FT                   /note="AdoMet-dependent heme synthase"
FT                   /id="PRO_0000450511"
FT   DOMAIN          34..257
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         50
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         54
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   BINDING         57
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
SQ   SEQUENCE   388 AA;  43266 MW;  1F93E41589994B7B CRC64;
     MHNANHPHGN GHPAEKKGMG AHSGAMNMPR TLEDGSPACR LIAWEVTRSC NLACKHCRAE
     AHTEPYPGEL STQEAKALID TFPEVGNPII IFTGGDPMMR ADLYELIRYA TGLGLRCVLS
     PNGTLITGQN AVQIREAGVQ RCSISIDGPS AELHDEFRGV PGAFEQSMRG IEFLKQAGVE
     FQINTTVTRD NLPYFKDIFK LCENLGAAAW HIFLLVPTGR AAQLGAQVIT AEEYEEVLNW
     FYDFRKTTSM HLKATCAPHY YRIMRQRAKE EGLPVTPDNF GMDAMTRGCL GGIGFCFISH
     TGQVQPCGYL ELDCGNVRDT RFPEIWRKSE YFRQFRTPEE YDGKCGHCEY HNVCGGCRAR
     GFTMSGSHMA EEPLCTYQPR KKPAADRK