AHBC_METBF
ID AHBC_METBF Reviewed; 399 AA.
AC Q46BK8;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Fe-coproporphyrin III synthase {ECO:0000305};
DE EC=4.1.3.- {ECO:0000269|PubMed:21969545, ECO:0000269|PubMed:24669201};
GN Name=ahbC {ECO:0000303|PubMed:21969545};
GN OrderedLocusNames=Mbar_A1793 {ECO:0000312|EMBL:AAZ70734.1};
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, AND CATALYTIC ACTIVITY.
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, 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 didecarboxysiroheme into Fe-coproporphyrin III by
CC oxidative loss of two acetic acid side chains.
CC {ECO:0000269|PubMed:21969545, ECO:0000269|PubMed:24669201}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=12,18-didecarboxysiroheme + 2 AH2 + 2 S-adenosyl-L-methionine
CC = 2 5'-deoxyadenosine + 2 A + 2 acetate + Fe-coproporphyrin III + 2
CC H(+) + 2 L-methionine; Xref=Rhea:RHEA:37431, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:68438, ChEBI:CHEBI:140497;
CC Evidence={ECO:0000269|PubMed:21969545, ECO:0000269|PubMed:24669201};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01266};
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; AAZ70734.1; -; Genomic_DNA.
DR RefSeq; WP_011306780.1; NC_007355.1.
DR AlphaFoldDB; Q46BK8; -.
DR SMR; Q46BK8; -.
DR STRING; 269797.Mbar_A1793; -.
DR EnsemblBacteria; AAZ70734; AAZ70734; Mbar_A1793.
DR GeneID; 3625155; -.
DR KEGG; mba:Mbar_A1793; -.
DR eggNOG; arCOG00938; Archaea.
DR HOGENOM; CLU_009273_4_0_2; -.
DR OMA; PVVIWNL; -.
DR OrthoDB; 18533at2157; -.
DR BioCyc; MetaCyc:MON-18866; -.
DR UniPathway; UPA00252; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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; IPR030894; Ahb_Proteobacteria.
DR InterPro; IPR034479; AhbC-like.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR017200; PqqE-like.
DR InterPro; IPR007197; rSAM.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF13186; SPASM; 1.
DR PIRSF; PIRSF037420; PQQ_syn_pqqE; 1.
DR SFLD; SFLDF00543; alternative_heme_biosynthesis; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR04546; rSAM_ahbC_deAc; 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; Lyase; Metal-binding;
KW S-adenosyl-L-methionine.
FT CHAIN 1..399
FT /note="Fe-coproporphyrin III synthase"
FT /id="PRO_0000450510"
FT DOMAIN 36..253
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
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 399 AA; 45108 MW; 0C973632E9437124 CRC64;
MIGISKLYCG TVEPSDALRY GRDSKKLPSH LLQFSKDKKP VVVWNMTRRC NLKCVHCYAQ
AKDIEFENEL STEEGKALID DLASFGSPVI LFSGGEPTMR KDLPELAAYA REKGMRAVIS
TNGTLIDREM AKKLKEVGLS YVGVSLDGIR ETNDKFRGMK GAFDAALRGL HNCQEEGIKV
GLRFTINKQN VRDIPAIFDL LEEEKIPRIC FYHLVYAGRG SKMVNEDLSL EESRQAVDLI
LERTRKLHEK GFPAEVLTVD NHCDGPYLYM KLLKENPERA AEVFELLSMN QGNSSGIGIG
CVSWDGAVHA DQFWRHYSFG NVRERPFSEI WTDLSDELMA GLKNRKPLIK AHADRCARCK
WLDVCNGNFR VRAEAVYGNV WADDPACYLT KEEIGYYEA
