ID A0A024FGG5_9FLAO Unreviewed; 377 AA.
AC A0A024FGG5;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN ORFNames=WPG_1719 {ECO:0000313|EMBL:BAO75949.1};
OS Winogradskyella sp. PG-2.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=754409 {ECO:0000313|EMBL:BAO75949.1, ECO:0000313|Proteomes:UP000031636};
RN [1] {ECO:0000313|EMBL:BAO75949.1, ECO:0000313|Proteomes:UP000031636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG-2 {ECO:0000313|EMBL:BAO75949.1,
RC ECO:0000313|Proteomes:UP000031636};
RX PubMed=24874677; DOI=10.1128/genomeA.00490-14;
RA Kumagai Y., Yoshizawa S., Oshima K., Hattori M., Iwasaki W., Kogure K.;
RT "Complete Genome Sequence of Winogradskyella sp. Strain PG-2, a
RT Proteorhodopsin-Containing Marine Flavobacterium.";
RL Genome Announc. 2:e00490-14(2014).
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; AP014583; BAO75949.1; -; Genomic_DNA.
DR RefSeq; WP_045471256.1; NZ_AP014583.1.
DR AlphaFoldDB; A0A024FGG5; -.
DR STRING; 754409.WPG_1719; -.
DR KEGG; win:WPG_1719; -.
DR HOGENOM; CLU_027579_2_2_10; -.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000031636; Chromosome.
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 CDD; cd01335; Radical_SAM; 1.
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; SFLDG01065; anaerobic_coproporphyrinogen-I; 1.
DR SFLD; SFLDF00562; HemN-like__clustered_with_heat; 1.
DR SFLD; SFLDF00288; HemN-like__clustered_with_nucl; 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:UP000031636};
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 377 AA; 43162 MW; 3C823D27033F08A9 CRC64;
MAGIYIHIPF CKQACHYCDF HFSTSLKKKD DLINALTKEL ELRKEEFKDI TIETIYFGGG
TPSLLTNNEL QFLIDAVYKH YKVSNNPEIT LEANPDDLSK NRIIELSKSP INRLSIGIQS
FFEADLKLMN RAHNAEEAKA CLEEATKHFD NISLDLIYGI PGSTNAQWNE NIETALSYNV
PHISSYALTV EPKTALASFI KKGIIDNVDD EQAHEQFHIL KEKLEDEGFM HYELSNFGKD
NFFSRNNSAY WKGKSYIGIG PSAHSFNGKQ RGWNVSNNSK YIKAIQQNEL PIEIEILTLT
DQYNEYVMTG LRTIWGVSFL KVENDFGIVF KDYLIEQSEV FINQHLLYID DEHLRVTKKG
QFLSDGIASE LFKLNLS
//