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Database: UniProt
Entry: K0IXU7_AMPXN
LinkDB: K0IXU7_AMPXN
Original site: K0IXU7_AMPXN 
ID   K0IXU7_AMPXN            Unreviewed;       386 AA.
AC   K0IXU7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN   Name=hemN {ECO:0000313|EMBL:BAM47229.1};
GN   OrderedLocusNames=AXY_10970 {ECO:0000313|EMBL:BAM47229.1};
OS   Amphibacillus xylanus (strain ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667
OS   / NBRC 15112 / Ep01).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Amphibacillus.
OX   NCBI_TaxID=698758 {ECO:0000313|EMBL:BAM47229.1, ECO:0000313|Proteomes:UP000006294};
RN   [1] {ECO:0000313|EMBL:BAM47229.1, ECO:0000313|Proteomes:UP000006294}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667 / NBRC 15112 /
RC   Ep01 {ECO:0000313|Proteomes:UP000006294};
RA   Nakazawa H., Katano Y., Nakamura S., Sasagawa M., Fukada J., Arai T.,
RA   Sasakura N., Mochizuki D., Hosoyama A., Harada K., Horikawa H., Kato Y.,
RA   Harada T., Sasaki K., Sekiguchi M., Hodoyama M., Nishiko R., Narita H.,
RA   Hanamaki A., Hata C., Konno Y., Niimura Y., Yamazaki S., Fujita N.;
RT   "Whole genome sequence of Amphibacillus xylinus NBRC 15112.";
RL   Submitted (JAN-2011) 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}.
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DR   EMBL; AP012050; BAM47229.1; -; Genomic_DNA.
DR   RefSeq; WP_015009834.1; NC_018704.1.
DR   AlphaFoldDB; K0IXU7; -.
DR   STRING; 698758.AXY_10970; -.
DR   KEGG; axl:AXY_10970; -.
DR   PATRIC; fig|698758.3.peg.1094; -.
DR   eggNOG; COG0635; Bacteria.
DR   HOGENOM; CLU_027579_2_2_9; -.
DR   OrthoDB; 9808022at2; -.
DR   Proteomes; UP000006294; 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; RADICAL S-ADENOSYL METHIONINE DOMAIN-CONTAINING PROTEIN 1, MITOCHONDRIAL; 1.
DR   Pfam; PF06969; HemN_C; 1.
DR   Pfam; PF04055; Radical_SAM; 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   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|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   Oxidoreductase {ECO:0000313|EMBL:BAM47229.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006294};
KW   S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT   DOMAIN          1..232
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   386 AA;  45128 MW;  86453D3007FD3554 CRC64;
     MITSAYIHIP FCEKICHYCD FTKFFYQEKM ADEYLAALAN EINFYLSDKK HTMRTIFVGG
     GTPTALNLAQ LEYLLQTIDK HMDVPNVEEY TFEANPGDLN EDKIKLLRMY GVNRISMGVQ
     SFDNQLLEDL GRLHRVKDVE ENINHLIKHG LTNISIDLMY GLPNQTIEIF NDSIEKALSF
     DLPHYSTYSL QIEPKTVFYQ RHQKGKLHKP PEEVEASMFE LLIEKMKQHG KFQYEVSNFA
     EPGYESKHNL TYWDNNYYYG FGAGASGYLP GKRHINLRPF PAYVKEANAS GQPILHIDEV
     GKKEQIEEEM FLGLRKRTGV NKNAFKQKYN VTIDQIYQEQ IHDLIARNWL EETSDYVRMT
     EKGQLFGNEV FQRFLLDDQE FNDLFK
//
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