AHBD_METBF
ID AHBD_METBF Reviewed; 349 AA.
AC Q46CH7;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=AdoMet-dependent heme synthase {ECO:0000305};
DE EC=1.3.98.6 {ECO:0000269|PubMed:24669201};
GN Name=ahbD {ECO:0000303|PubMed:24669201};
GN OrderedLocusNames=Mbar_A1458 {ECO:0000312|EMBL:AAZ70415.1};
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, COFACTOR, AND PATHWAY.
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).
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:24669201}.
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:24669201};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:24669201};
CC Note=May bind 2 [4Fe-4S] clusters. {ECO:0000269|PubMed:24669201};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000269|PubMed:24669201}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. {ECO:0000305}.
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DR EMBL; CP000099; AAZ70415.1; -; Genomic_DNA.
DR RefSeq; WP_011306461.1; NC_007355.1.
DR AlphaFoldDB; Q46CH7; -.
DR SMR; Q46CH7; -.
DR STRING; 269797.Mbar_A1458; -.
DR EnsemblBacteria; AAZ70415; AAZ70415; Mbar_A1458.
DR GeneID; 3627739; -.
DR KEGG; mba:Mbar_A1458; -.
DR eggNOG; arCOG00938; Archaea.
DR HOGENOM; CLU_009273_4_0_2; -.
DR OMA; AMWEVFF; -.
DR OrthoDB; 18533at2157; -.
DR BRENDA; 1.3.98.6; 3250.
DR UniPathway; UPA00252; -.
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; S-adenosyl-L-methionine.
FT CHAIN 1..349
FT /note="AdoMet-dependent heme synthase"
FT /id="PRO_0000450513"
FT DOMAIN 5..214
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 19
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 23
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 26
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 349 AA; 38631 MW; 9EC7D01D81368167 CRC64;
MIAMTNAPRL IAWELTAGCN LNCVHCRGAS TSSVPAGELT TDEAKHFIDE VASIGKPILI
LSGGEPLTRP DVFEIARYGT DAGLRVVLAT NGTLLTPEIV EKLRAAGVQR LSVSIDGANA
ETHDNFRGMP GAFERTLAGI EVLRKADFPF QINTTVSKRN LEEITKTFEL AKELGAVAYH
VFFLVPTGRG DESDEVSPAD YERILHWFYE MQKESKIQLK ATCAPHYFRI MRQQAKKEGI
EISVKTHGYE AMTKGCLGGT GFCFVSSVGK VFPCGYLPVL AGNIREQPFR EIWENAEVFR
KLRDPEELKG KCGICEYKKV CAGCRARAYA ATGDYLEEEP YCIYRPGKK
