GenomeNet

Database: UniProt
Entry: A0A2P8H4U5_9BACL
LinkDB: A0A2P8H4U5_9BACL
Original site: A0A2P8H4U5_9BACL 
ID   A0A2P8H4U5_9BACL        Unreviewed;       379 AA.
AC   A0A2P8H4U5;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Heme chaperone HemW {ECO:0000256|ARBA:ARBA00017228, ECO:0000256|RuleBase:RU364116};
GN   ORFNames=B0H99_103360 {ECO:0000313|EMBL:PSL41224.1};
OS   Planomicrobium soli.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planomicrobium.
OX   NCBI_TaxID=1176648 {ECO:0000313|EMBL:PSL41224.1, ECO:0000313|Proteomes:UP000242682};
RN   [1] {ECO:0000313|EMBL:PSL41224.1, ECO:0000313|Proteomes:UP000242682}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12259 {ECO:0000313|EMBL:PSL41224.1,
RC   ECO:0000313|Proteomes:UP000242682};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (MAR-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:PSL41224.1}.
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; PYAT01000003; PSL41224.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P8H4U5; -.
DR   OrthoDB; 9808022at2; -.
DR   Proteomes; UP000242682; 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; 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|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          1..234
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   379 AA;  43317 MW;  A4E81699AF1D96D9 CRC64;
     MVKGLYIHIP FCHQICHYCD FNKVFFKDQP VDAYIDSLGK ELALWKQEGA LDQPLETVFL
     GGGTPTSLTP QQLETLLGYI HRYVPMADNL EWTSEANPDE LTKEKMQVLF DGGVNRLSMG
     VQSFDEDLLK RLGRTHSNGD VARAVESARQ VGFTNLSFDL MYGLPGQSME QWNDTLEKAF
     AFDLPHFSAY SLIIEPKTVF YNLMTKGKLN TVTEDLEADM YDKLMDEMDI RGLKQYEISN
     FARPNFESRH NLLYWDNAEY IGVGAGAHGY VNGIRYSNAG PLKKYMAPLE EGKRPLLNTH
     EVPVNEQMEE EMFLGLRKTA GVSLSGFQKK FQRPIEEIYD AIVKKEIDKK NLVIEQDFIK
     LTRKGRFVGN EVFEQFLLG
//
DBGET integrated database retrieval system