ID A0A368N3F2_9FLAO Unreviewed; 374 AA.
AC A0A368N3F2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN ORFNames=DQ356_00480 {ECO:0000313|EMBL:RCU44736.1};
OS Chryseobacterium lacus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=2058346 {ECO:0000313|EMBL:RCU44736.1, ECO:0000313|Proteomes:UP000252172};
RN [1] {ECO:0000313|EMBL:RCU44736.1, ECO:0000313|Proteomes:UP000252172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLOS41 {ECO:0000313|EMBL:RCU44736.1,
RC ECO:0000313|Proteomes:UP000252172};
RA Li C.-M.;
RT "Chryseobacterium lacus sp. nov., isolated from lake water.";
RL Submitted (JUL-2018) 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:RCU44736.1}.
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DR EMBL; QPIE01000001; RCU44736.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368N3F2; -.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000252172; 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; 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; 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:UP000252172};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 1..229
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 374 AA; 42742 MW; 61BC5C7D55F89A69 CRC64;
MIYVHIPFCR QKCSYCNFHF STSLSLKDEI LKALKKEIGL RKNELNLANL KSLYFGGGTP
SILTPEEIMM LTDEVLKYFH FDPDIEITLE ANPDDLNKDF LSGLSKTVVN RLSIGTQSFH
DEDLKLMNRI HSGAEAEDSI KRAQDHGFHN ISLDLIYGSP VSDFEVWKNN LRKAVALEVP
HISSYALTVE PKTALNSWIK TKKVPSPKDE EQQKEFHYMS DFLKDNGFIH YEISNFAKPG
FYSRHNTAYW NNEPYLGIGP SAHSYNGRDK RSWNVANNTL YIKSLAENKF PSETEILSEK
DRYNEIIMTG LRTASGVNIA RLEESFSSEI LDHFEKELTK GLQSGVLKTT ENHLMIPEEN
WFLADGIASD LFIL
//
