ID A0A1W6SLK1_9PROT Unreviewed; 406 AA.
AC A0A1W6SLK1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN ORFNames=EBAPG3_002230 {ECO:0000313|EMBL:ARO86686.1};
OS Nitrosospira lacus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=1288494 {ECO:0000313|EMBL:ARO86686.1, ECO:0000313|Proteomes:UP000012179};
RN [1] {ECO:0000313|EMBL:ARO86686.1, ECO:0000313|Proteomes:UP000012179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APG3 {ECO:0000313|EMBL:ARO86686.1,
RC ECO:0000313|Proteomes:UP000012179};
RX PubMed=25336720; DOI=10.1099/ijs.0.070789-0;
RA Urakawa H., Garcia J.C., Nielsen J.L., Le V.Q., Kozlowski J.A., Stein L.Y.,
RA Lim C.K., Pommerening-Roser A., Martens-Habbena W., Stahl D.A., Klotz M.G.;
RT "Nitrosospira lacus sp. nov., a psychrotolerant, ammonia-oxidizing
RT bacterium from sandy lake sediment.";
RL Int. J. Syst. Evol. Microbiol. 65:242-250(2015).
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; CP021106; ARO86686.1; -; Genomic_DNA.
DR RefSeq; WP_040851515.1; NZ_CP021106.3.
DR AlphaFoldDB; A0A1W6SLK1; -.
DR KEGG; nlc:EBAPG3_002230; -.
DR eggNOG; COG0635; Bacteria.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000012179; 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; 3.30.750.200; -; 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 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; 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|RuleBase:RU364116};
KW Reference proteome {ECO:0000313|Proteomes:UP000012179};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 18..253
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 406 AA; 46027 MW; C8A48DA415A7C754 CRC64;
MTAIIPPAPR PGNQSPKLRS LPPLSLYIHI PWCMKKCPYC DFNSHEVRGG NSNVPEAEYV
SALIRDLETA LPQIWGRSVT SVFFGGGTPS LFSARSIDAI LTAVRTLLSL EHFAEITLEA
NPGTFEAGKF ADFRAAGVNR LSIGVQSFNP RHLQLLGRIH DGREARRAIE LAQENFDNVN
LDLMYALPHQ TMEEARCDIE TAAAYGVPHI SAYHLTLEPN TLFHRYPPPL PDNDLSAEMQ
MMIEQTLAQR GYLNYEISAF ARFGRESRHN MNYWLFGDYL GIGAGAHSKI SFDTRIVRQM
RYKQPRDYLA KTSLDMTALD SPFIMEQHEV GQHDRGFEFM MNALRLTGGF ETGMFVERTG
LSIGSIQRQL DEAERRQLIM RDYQRIAPTL TGRRFLNDLL QIFLPE
//