ID A0A370G4N9_GLULI Unreviewed; 400 AA.
AC A0A370G4N9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|ARBA:ARBA00017228, ECO:0000256|RuleBase:RU364116};
GN ORFNames=C7453_103213 {ECO:0000313|EMBL:RDI38752.1}, HLH32_07420
GN {ECO:0000313|EMBL:MBB2186216.1};
OS Gluconacetobacter liquefaciens (Acetobacter liquefaciens).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconacetobacter.
OX NCBI_TaxID=89584 {ECO:0000313|EMBL:RDI38752.1, ECO:0000313|Proteomes:UP000254958};
RN [1] {ECO:0000313|EMBL:RDI38752.1, ECO:0000313|Proteomes:UP000254958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5603 {ECO:0000313|EMBL:RDI38752.1,
RC ECO:0000313|Proteomes:UP000254958};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB2186216.1, ECO:0000313|Proteomes:UP000562982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 1382 {ECO:0000313|EMBL:MBB2186216.1,
RC ECO:0000313|Proteomes:UP000562982};
RA Sombolestani A.;
RT "Description of novel Gluconacetobacter.";
RL Submitted (APR-2020) 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 -!- 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:RDI38752.1}.
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DR EMBL; JABEQI010000003; MBB2186216.1; -; Genomic_DNA.
DR EMBL; QQAW01000003; RDI38752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370G4N9; -.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000254958; Unassembled WGS sequence.
DR Proteomes; UP000562982; 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; HEME CHAPERONE-RELATED; 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|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 S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 9..247
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 400 AA; 43597 MW; 5B4B183425E8EED3 CRC64;
MPSDAQAPAN EGAPLALYVH WPFCLAKCPY CDFNSHVRDT IPQARFSAAL RRELAHEAAR
LTEDGPRRLG SIFFGGGTPS LMAPETVAAL IADARSLFAT APDLEITLEA NPTSVEIERL
RAFRNAGINR VSLGIQSLDD DALHLLGRQH SAGQAIAALE TARDLFGRIS FDLIYARPNQ
SPAAWRAELN QALALVSDHL SLYQLTIEPG TRFEGLHRQG LLTLPDEDSG ALMYEETATV
AAGHGLAAYE VSNYARPGAE SRHNLTYWRY DDYLGIGPGA HGRTTLADGL HATRRHRAPE
PWTERVERTG SGLMQDDILT SRDRAREMLL MGLRLTEGVP EARFAQRTGM AMKDALDPTI
LAAALGEGYL VRDETIQGAV LRATNAGRLR LEALLGAMVL
//