ID F9VEK9_LACGL Unreviewed; 374 AA.
AC F9VEK9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN OrderedLocusNames=LCGL_1300 {ECO:0000313|EMBL:BAK60760.1};
OS Lactococcus garvieae (strain Lg2) (Enterococcus seriolicida).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=420890 {ECO:0000313|EMBL:BAK60760.1, ECO:0000313|Proteomes:UP000008520};
RN [1] {ECO:0000313|EMBL:BAK60760.1, ECO:0000313|Proteomes:UP000008520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lg2 {ECO:0000313|EMBL:BAK60760.1,
RC ECO:0000313|Proteomes:UP000008520};
RX PubMed=21829716; DOI=10.1371/journal.pone.0023184;
RA Morita H., Toh H., Oshima K., Yoshizaki M., Kawanishi M., Nakaya K.,
RA Suzuki T., Miyauchi E., Ishii Y., Tanabe S., Murakami M., Hattori M.;
RT "Complete genome sequence and comparative analysis of the fish pathogen
RT Lactococcus garvieae.";
RL PLoS ONE 6:E23184-E23184(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP009333; BAK60760.1; -; Genomic_DNA.
DR RefSeq; WP_014025039.1; NC_017490.1.
DR AlphaFoldDB; F9VEK9; -.
DR STRING; 420890.LCGL_1300; -.
DR KEGG; lgv:LCGL_1300; -.
DR PATRIC; fig|420890.5.peg.1288; -.
DR eggNOG; COG0635; Bacteria.
DR HOGENOM; CLU_027579_2_2_9; -.
DR OMA; HIPWCVR; -.
DR Proteomes; UP000008520; 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; HEME CHAPERONE-RELATED; 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364116};
KW Reference proteome {ECO:0000313|Proteomes:UP000008520};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 1..233
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 374 AA; 43222 MW; A2079A0C1820D8E6 CRC64;
MKNNETKAAY VHIPFCSHIC YYCDFAKVLM TGQPVEAYID ELLKEYDSYG ISSLQTLYIG
GGTPSVLPAD QLEKLLTHLT KNLDLEELEE FTVEANPSDL TDEVLAVLAQ SPVNRISLGV
QSFDDKLLKK IGRTHTEAQV YSSIERLRAA GFENITIDLI YGLPNQTMEM VERDVQKFLE
LDLPHVALYS LILEDHTVFM NRQRRGRLRL PSDDRNADMY EYIIETLTAK GYSHYEVSNF
GKIGYESKHN MTYWDNAEYY GVGAGASGYL EGIRYKNHGP VHHYLREENK RVNEEVLTRK
QRIEEEMFLG LRKKNGVSIE RFHKKFGQTL EEIYGTIIEE LTFQKMLFEA DGRIRMTEKG
FELGNEVFER FLLD
//