ID A0A139SHM7_9BACT Unreviewed; 392 AA.
AC A0A139SHM7;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN ORFNames=AXK12_08250 {ECO:0000313|EMBL:KXU34046.1};
OS Cephaloticoccus capnophilus.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC Cephaloticoccus.
OX NCBI_TaxID=1548208 {ECO:0000313|EMBL:KXU34046.1, ECO:0000313|Proteomes:UP000071392};
RN [1] {ECO:0000313|EMBL:KXU34046.1, ECO:0000313|Proteomes:UP000071392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CV41 {ECO:0000313|EMBL:KXU34046.1,
RC ECO:0000313|Proteomes:UP000071392};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably acts as a heme chaperone, transferring heme to an
CC unknown acceptor. Binds one molecule of heme per monomer, possibly
CC covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000256|RuleBase:RU364116}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU364116}.
CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase
CC family. HemW subfamily. {ECO:0000256|ARBA:ARBA00006100}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXU34046.1}.
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DR EMBL; LSZP01000062; KXU34046.1; -; Genomic_DNA.
DR RefSeq; WP_068713360.1; NZ_LSZP01000062.1.
DR AlphaFoldDB; A0A139SHM7; -.
DR STRING; 1548208.AXK12_08250; -.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000071392; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.750.200; -; 1.
DR InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR010723; HemN_C.
DR InterPro; IPR004559; HemW-like.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR00539; hemN_rel; 1.
DR PANTHER; PTHR13932; COPROPORPHYRINIGEN III OXIDASE; 1.
DR PANTHER; PTHR13932:SF5; RADICAL S-ADENOSYL METHIONINE DOMAIN-CONTAINING PROTEIN 1, MITOCHONDRIAL; 1.
DR Pfam; PF06969; HemN_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00562; HemN-like__clustered_with_heat; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|RuleBase:RU364116};
KW Chaperone {ECO:0000256|RuleBase:RU364116};
KW Cytoplasm {ECO:0000256|RuleBase:RU364116};
KW Heme {ECO:0000256|RuleBase:RU364116}; Iron {ECO:0000256|RuleBase:RU364116};
KW Iron-sulfur {ECO:0000256|RuleBase:RU364116};
KW Metal-binding {ECO:0000256|RuleBase:RU364116};
KW Reference proteome {ECO:0000313|Proteomes:UP000071392};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 4..237
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 392 AA; 42927 MW; C071FDF83AB9A3D5 CRC64;
MAAPNRAAPL GLYVHVPFCA STCDFCAFYQ VRPTASDIAD YFAACEAEAA LVKWSRPVTT
VFWGGGTPGL LSPDALRRLG EFTLRCCSET ECGSGPTEWT VEMAPASVTE ARLAALREIG
VTRISMGVQS FQAALLAALG RQHSREQIYR AYERIRAAGF SSVNLDLMFA LPGQTAAEWE
ADIAEALALA PDHLSTYCLT FEEDTALWLK LSQGRVKLDP EHEAQLYEQT WARLAAAGYG
QYEVANFARP GHACRHNLNT WAMSEWVGLG PAAASQHGGW RGGNVADLRG WAERVQRGER
MTEERKEMTP AALAEDAFIF GLRMNAGVSL EEWRTRAPDA PWAAVEALAE RLVADELALW
SDDRLCLSTR GRLLADAVGL EMMEAFQDAS QS
//
