ID A0A3G2G9P4_9FLAO Unreviewed; 374 AA.
AC A0A3G2G9P4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN Name=hemW {ECO:0000313|EMBL:AYN01405.1};
GN ORFNames=EAG08_14795 {ECO:0000313|EMBL:AYN01405.1};
OS Chryseobacterium sp. 3008163.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=2478663 {ECO:0000313|EMBL:AYN01405.1, ECO:0000313|Proteomes:UP000273471};
RN [1] {ECO:0000313|EMBL:AYN01405.1, ECO:0000313|Proteomes:UP000273471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3008163 {ECO:0000313|EMBL:AYN01405.1};
RA Bekkelund A.K., Hansen B.R., Stokken H., Eriksen B.F., Kashulin N.A.;
RT "Effects of UV and annual dynamics of microbial communities in freshwater
RT RAS systems.";
RL Submitted (OCT-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}.
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DR EMBL; CP033070; AYN01405.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G2G9P4; -.
DR KEGG; chrs:EAG08_14795; -.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000273471; 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; 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:UP000273471};
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; 43419 MW; 2795DF3D6783E8DC CRC64;
MIYIHIPFCK QKCSYCNFHF STSLNFKDEM IAAMKKEIFL RKDELQSKNL QSLYFGGGTP
SILSGDEIKS LIDEVLKYFS FNADIEITLE ANPDDLDKNF LRQLSNSPIN RLSIGTQSFF
DEDLRLMNRA HNASDAEGSI KRAQDFGFEN LSIDLIYGSP TSNLEIWKQN LNKTIALEVP
HISSYALTVE PKTALEKWIA NGKVSNPKEE EQNREFYYMI DFLKDHEFEH YEISNFAKKG
FHSRHNSAYW KYNEYLGIGP SAHSYNGFDV RSWNIANNQQ YIKKLNSKLL AKETEILSPK
DQFNEMIMIG LRTTWGVDLE SLKNKFKEDI LDQFHKELQQ KIADGILMKE NNHLKIPEKH
WFMADGIASD LFQV
//
