ID A0A1M6APV2_9FLAO Unreviewed; 383 AA.
AC A0A1M6APV2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN ORFNames=SAMN05216261_0539 {ECO:0000313|EMBL:SHI38233.1};
OS Algibacter luteus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Algibacter.
OX NCBI_TaxID=1178825 {ECO:0000313|EMBL:SHI38233.1, ECO:0000313|Proteomes:UP000184396};
RN [1] {ECO:0000313|EMBL:SHI38233.1, ECO:0000313|Proteomes:UP000184396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12213 {ECO:0000313|EMBL:SHI38233.1,
RC ECO:0000313|Proteomes:UP000184396};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQYK01000001; SHI38233.1; -; Genomic_DNA.
DR RefSeq; WP_019386126.1; NZ_FQYK01000001.1.
DR AlphaFoldDB; A0A1M6APV2; -.
DR STRING; 1178825.SAMN05216261_0539; -.
DR eggNOG; COG0635; Bacteria.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000184396; 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; 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:UP000184396};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 1..236
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 383 AA; 43644 MW; 8DA1353917AB2332 CRC64;
MAGIYIHIPF CKQACHYCDF HFSTSLKKKD ELLQALIQEL VLRKGELKNI SVETIYFGGG
TPSLLSINEL KLLIDSVFKN YTVVENPEIT LEANPDDLIT VQGQSKTIFE EYKSIGINRL
SIGIQSFFER DLKLMNRAHN AHEAKDCLTL ATKYFDNISV DLIYGIPGLT NNEWIENIDT
VLAFNIPHIS CYALTVEPKT ALESFIKKGL IDNVDDDLAQ EQFNILVDKL EANGFVNYEL
SNFGKSNYFS KNNSAYWQGK PYLGIGPSAH SFNGDQRSWN VSNNTKYIKS IQLNELPREV
EILSKTDKFN EYIMTGLRTI WGVSLEKVEE NFGITYKNHL LQQAEIYIKE QLLYIEKDNL
LTTKKGKFLS DGIASNLFKI NLI
//
