ID A0A1Y5T348_9RHOB Unreviewed; 372 AA.
AC A0A1Y5T348;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|ARBA:ARBA00017228, ECO:0000256|RuleBase:RU364116};
GN Name=hemN_2 {ECO:0000313|EMBL:SLN51241.1};
GN ORFNames=PAM7066_02329 {ECO:0000313|EMBL:SLN51241.1};
OS Palleronia marisminoris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Palleronia.
OX NCBI_TaxID=315423 {ECO:0000313|EMBL:SLN51241.1, ECO:0000313|Proteomes:UP000193870};
RN [1] {ECO:0000313|EMBL:SLN51241.1, ECO:0000313|Proteomes:UP000193870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7066 {ECO:0000313|EMBL:SLN51241.1,
RC ECO:0000313|Proteomes:UP000193870};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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; FWFV01000006; SLN51241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5T348; -.
DR STRING; 315423.SAMN04488020_10696; -.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000193870; 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; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
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; SFLDG01065; anaerobic_coproporphyrinogen-I; 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|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU364116};
KW Cytoplasm {ECO:0000256|RuleBase:RU364116};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU364116};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU364116};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU364116};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364116};
KW Oxidoreductase {ECO:0000313|EMBL:SLN51241.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193870};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 1..234
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 372 AA; 40704 MW; 76C17065B49C0420 CRC64;
MNRVGLYIHW PFCQAKCPYC DFNSHVVSGI DQARWRAAFA REIARYRDEM PDAVIGSIFF
GGGTPSLMEV ETVASIIDAT QKAWRFANDV EITLEANPTS VEAERFRGYR TAGVNRISIG
IQALNDPDLR KLGRLHSVSE AEAAFTVARE NFPRVSFDLI YARQDQSLAA WEAELGRALG
LAADHLSLYQ LTIEPGTAFG DRFDRGKLPG LPDEDLAADM FELTQDMTAG AGLPAYEVSN
HAALDAESRH NMIYWTGGEY IGIGPGAHGR LSAPLGRIAT EALMAPGGWL NAVERGKGYE
TRTELSAREI AEERIMMGLR LRSGVDLAGL DASLGDTRNL EELGLLVRTA DRLVLTPAGR
PLLNAVLREL LA
//
