ID A0A1T5EVJ4_9FLAO Unreviewed; 345 AA.
AC A0A1T5EVJ4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN ORFNames=SAMN05660477_01622 {ECO:0000313|EMBL:SKB87967.1};
OS Soonwooa buanensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Soonwooa.
OX NCBI_TaxID=619805 {ECO:0000313|EMBL:SKB87967.1, ECO:0000313|Proteomes:UP000191112};
RN [1] {ECO:0000313|EMBL:SKB87967.1, ECO:0000313|Proteomes:UP000191112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22323 {ECO:0000313|EMBL:SKB87967.1,
RC ECO:0000313|Proteomes:UP000191112};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUYZ01000004; SKB87967.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5EVJ4; -.
DR STRING; 619805.SAMN05660477_01622; -.
DR Proteomes; UP000191112; 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 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:UP000191112};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 1..200
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 345 AA; 39803 MW; 474D64E7C79ECE3E CRC64;
MLSSIIKEFS LRHQELENKK IDSLYFGGGT PSILEAKEIG KIIDEANRYF EFNPDMELTL
EANPDDLNAS FLKEIKNIGI NRLSIGTQSF FEDDLKLMNR AHTASEAESS IKRAQDFGLE
NISVDLIYGS PTSTMEQWKQ NLAKIIELQV PHVSSYALTI ESKTILDNWI NQQKIKSPDE
AFQNDAFFYM SEFLKENGFD HYEISNFGKP NFHSKHNSSY WEYKEYLGIG PSAHSYDGKN
LRSWNVANNT KYIKSLSENQ LPIEREELNE NDRYNEMLMI GLRTQKGVDL MRFKNSFSSE
MISAFENSIQ QKIKDGILKI ENNRLIIPEQ HWFMADGIAA DLFLV
//
