ID A0A1G6Z283_9FLAO Unreviewed; 378 AA.
AC A0A1G6Z283;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN ORFNames=SAMN05421636_102460 {ECO:0000313|EMBL:SDD96651.1};
OS Pricia antarctica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Pricia.
OX NCBI_TaxID=641691 {ECO:0000313|EMBL:SDD96651.1, ECO:0000313|Proteomes:UP000199109};
RN [1] {ECO:0000313|EMBL:SDD96651.1, ECO:0000313|Proteomes:UP000199109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23421 {ECO:0000313|EMBL:SDD96651.1,
RC ECO:0000313|Proteomes:UP000199109};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FNAO01000002; SDD96651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6Z283; -.
DR STRING; 641691.SAMN05421636_102460; -.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000199109; 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; 3.80.30.20; tm_1862 like domain; 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 InterPro; IPR023404; rSAM_horseshoe.
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; SFLDF00288; HemN-like__clustered_with_nucl; 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:UP000199109};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 1..230
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 378 AA; 42699 MW; C76C0FD2C68A4D2E CRC64;
MSGIYIHIPF CKQACHYCDF HFSTVMGKKE AMVSALQKEL VLRRDEFSDE VVETIYFGGG
TPSVLTVDEI QSIIETVYTN FEVSDSPEIT LEANPDDLSL EKIETLAASP LNRLSVGVQS
FFEADLKLMN RAHNAEEAEG CIRLAKKYFD NISIDLIYGI PDMSNARWKQ NIEKALFLDI
PHISSYALTV EPNTALANFI KKGIIKNVDD EVAQAHFHIL SETLEAAGFK SYEISNFGQP
GYFSRNNTAY WQQKKYIGIG PSAHSFDGLR RGWNINNNPK YLKAIESGEL PMETEILSTT
DKYNEYVMTG LRTIWGVSLD RISSEYGTKY REYLLKQAKK HREGQLLYLD GDLLLTTKKG
QFLADGIASD LFMLNLGQ
//
