ID A0A1I7BAN2_9FLAO Unreviewed; 375 AA.
AC A0A1I7BAN2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN ORFNames=SAMN05216474_2628 {ECO:0000313|EMBL:SFT84243.1};
OS Lishizhenia tianjinensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Crocinitomicaceae; Lishizhenia.
OX NCBI_TaxID=477690 {ECO:0000313|EMBL:SFT84243.1, ECO:0000313|Proteomes:UP000236454};
RN [1] {ECO:0000313|EMBL:SFT84243.1, ECO:0000313|Proteomes:UP000236454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7005 {ECO:0000313|EMBL:SFT84243.1,
RC ECO:0000313|Proteomes:UP000236454};
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; FPAS01000005; SFT84243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7BAN2; -.
DR STRING; 477690.SAMN05216474_2628; -.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000236454; 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; 3.80.30.20; tm_1862 like domain; 1.
DR InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
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; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01065; anaerobic_coproporphyrinogen-I; 1.
DR SFLD; SFLDG01082; B12-binding_domain_containing; 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:UP000236454};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 1..231
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 375 AA; 43015 MW; F7A4710C096AE19E CRC64;
MAGIYIHIPF CKQACSYCDF HFSTSFEKYR TRMVKAICKE IEVRKSYLKA EEIFSIYFGG
GTPSVLNAEE IRQLVDSILS NFKVNPKSEI TLEANPDDIN AERLEDWKKA GVNRLSIGVQ
SFRKQDLDWM NRAHTVEEAK SALRLAANYG FELSIDVIYG LPNFTLEDFK NNLDQVLHFS
PAHLSAYCLT VEENTALHKA VEQGKIVPAN NEAQSEQFDF LVAYLQAKGY EQYEISNFAR
EEKYAVHNSN YWKGEKYLGV GPSAHSFDGY TRSWNIANNA KYMKAIENQE DFYEVEELSI
YDQFNEALLV GLRTKWGVAK HRLPKELLNT EEFRQGIEEF KAEGYLLETE EVFLLTQKGR
LKADGIASDL FILAD
//
