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Database: UniProt
Entry: A0A0F6TST8_9GAMM
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ID   A0A0F6TST8_9GAMM        Unreviewed;       408 AA.
AC   A0A0F6TST8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Heme chaperone HemW {ECO:0000256|ARBA:ARBA00017228, ECO:0000256|RuleBase:RU364116};
GN   ORFNames=TQ33_2140 {ECO:0000313|EMBL:AKE53067.1};
OS   Kangiella geojedonensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Kangiellales; Kangiellaceae;
OC   Kangiella.
OX   NCBI_TaxID=914150 {ECO:0000313|EMBL:AKE53067.1, ECO:0000313|Proteomes:UP000034071};
RN   [1] {ECO:0000313|EMBL:AKE53067.1, ECO:0000313|Proteomes:UP000034071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCS-5 {ECO:0000313|EMBL:AKE53067.1,
RC   ECO:0000313|Proteomes:UP000034071};
RA   Kim K.M.;
RT   "Complete genome sequence of Kangiella geojedonensis strain YCS-5T.";
RL   Submitted (FEB-2015) 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}.
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DR   EMBL; CP010975; AKE53067.1; -; Genomic_DNA.
DR   RefSeq; WP_046562055.1; NZ_CP010975.1.
DR   AlphaFoldDB; A0A0F6TST8; -.
DR   STRING; 914150.TQ33_2140; -.
DR   KEGG; kge:TQ33_2140; -.
DR   PATRIC; fig|914150.5.peg.2169; -.
DR   HOGENOM; CLU_027579_2_1_6; -.
DR   OrthoDB; 9808022at2; -.
DR   Proteomes; UP000034071; 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; 3.20.20.70; 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   Reference proteome {ECO:0000313|Proteomes:UP000034071};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU364116}.
FT   DOMAIN          1..243
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   408 AA;  46030 MW;  FAE40013DC7EAEA5 CRC64;
     MLTNPPLSLY IHIPWCVRKC PYCDFNSHAI KNIKSDSQTE FDLPEKAYID RLIEDLEHEL
     PKVWGRRLHS IFIGGGTPSL FSPESLDRLI SAVRARLPFE NDIEITMEAN PGTFEAEKFR
     GFRQAGINRL SIGVQSFNAQ HLEQLGRIHN PEQAIAAAEF AHEAGYDSFN LDLMHGLPNQ
     TVEQALNDLG TAIRLKPHHI SWYQLTLEPN TLFHQQPPQL PHDEVLWDIQ EAGQALLAQH
     GYEQYETSAY AKSPRLRAKH NLNYWRFGDY LGIGAGAHGK ITRLDLGEVH RTTKKRHPKD
     YLNGSTASIS TDTPIPAHEL PFEFMLNALR LIDGVPTNLF SQYTGLPLSS IRATLEQAVD
     DGLLEDITTQ LKPSDKGALF LNELLERFIP SDNSKPEKGS ASIQFKQL
//
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