ID A0A1B9DPU4_9FLAO Unreviewed; 406 AA.
AC A0A1B9DPU4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN ORFNames=FBGL_10920 {ECO:0000313|EMBL:OCB71718.1};
OS Flavobacterium glycines.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=551990 {ECO:0000313|EMBL:OCB71718.1, ECO:0000313|Proteomes:UP000093226};
RN [1] {ECO:0000313|Proteomes:UP000093226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105008 {ECO:0000313|Proteomes:UP000093226};
RA Shin S.-K., Yi H.;
RT "Draft genome sequence of Paenibacillus glacialis DSM 22343.";
RL Submitted (MAR-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:OCB71718.1}.
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DR EMBL; LVEO01000018; OCB71718.1; -; Genomic_DNA.
DR RefSeq; WP_066328426.1; NZ_LVEO01000018.1.
DR AlphaFoldDB; A0A1B9DPU4; -.
DR STRING; 551990.SAMN05192550_0180; -.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000093226; 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 CDD; cd01335; Radical_SAM; 1.
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 S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 1..248
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 406 AA; 46864 MW; EF26586E955310A0 CRC64;
MSGIYIHIPF CKQACHYCDF HFSISMKKKD EMVLALAKEI ELRKNEFKDE VVETIYFGGG
TPSVLQISDL RLLIDAIYKN YIVSENPEIT LEANPDDLHL DFARCDNESE LSVRAESRTI
FEEYRSIGIN RLSIGIQSFF EDDLKMMNRA HNSEEAKKCL EIATKYFDNI SLDLIYGIPR
MSDERWKQNI ETALSFGVPH ISSYALTVEP KTALNKLIQT GKIAEPKDEV ASAHFMILME
TLEANGFLHY ELSNFGKPDY FSKNNSAYWL GKKYIGIGPS AHSYDGISRS WNIANNTLYL
KAIKENRLPN EIEILSVSDR YNEYIMTGLR TIWGVSLERI QSEFGQNYLD YLLKQAQKFL
SDDLLFIENN ILRPTKKGKF LTDGIASDLF YLIWNRSNHQ EHKEEL
//
