ID F7RPV1_9GAMM Unreviewed; 681 AA.
AC F7RPV1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Methylcrotonyl-CoA carboxylase biotin-containing subunit {ECO:0000313|EMBL:EGM69550.1};
DE EC=6.4.1.4 {ECO:0000313|EMBL:EGM69550.1};
GN ORFNames=SOHN41_02393 {ECO:0000313|EMBL:EGM69550.1};
OS Shewanella sp. HN-41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=327275 {ECO:0000313|EMBL:EGM69550.1, ECO:0000313|Proteomes:UP000002956};
RN [1] {ECO:0000313|EMBL:EGM69550.1, ECO:0000313|Proteomes:UP000002956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HN-41 {ECO:0000313|EMBL:EGM69550.1,
RC ECO:0000313|Proteomes:UP000002956};
RX PubMed=21868804; DOI=10.1128/JB.05578-11;
RA Kim D.H., Jiang S., Lee J.H., Cho Y.J., Chun J., Choi S.H., Park H.S.,
RA Hur H.G.;
RT "Draft Genome Sequence of Shewanella sp. Strain HN-41, Which Produces
RT Arsenic-Sulfide Nanotubes.";
RL J. Bacteriol. 193:5039-5040(2011).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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:EGM69550.1}.
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; AFOZ01000030; EGM69550.1; -; Genomic_DNA.
DR RefSeq; WP_007649004.1; NZ_AFOZ01000030.1.
DR AlphaFoldDB; F7RPV1; -.
DR STRING; 327275.SOHN41_02393; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000002956; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.40; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EGM69550.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..447
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 585..662
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 681 AA; 74049 MW; 36A9EE37DCD52E66 CRC64;
MFTKLLIANR GEIACRIIKT AQAMGVRTVA LYSDADKNAR HVAMADESFY LGGSAPADSY
LKGDLIIDIA KKSGAQAIHP GYGFLSENAG FARQCEAAGI VFVGPGSDAI DAMGSKSAAK
AIMTAANVPL VPGYHGDDQS DATLKAEALK IGFPMLIKAA YGGGGKGMRI VENENEIMEA
VNSARREAAS SFGNDKLLME RYLLKPRHVE VQVFADTFGN AIYLSDRDCS IQRRHQKVVE
EAPAPGLSDA LRTQMGEAAV AAAKAIDYVG AGTVEFLLDT DNSFYFMEMN TRLQVEHPVT
EMVTCQDLVK WQLMVASGQP LPLKQEEVRI HGHSFEVRIY AEDPQNAFLP ASGKLNFLRE
PEQSKHVRID SGIRENDVIS NFYDPMIAKL IVWDESRPRA LQRLVHALES YQISGLKHNI
EFLANIAEHP AFANADFSTD FIGRYGDALI GSPSSEADNA IAFAALYQVL ARKEAAKAQA
LNSADPYSPW GQVSGFRLNS CSQHSIALLN DAHELQQLVM LDLGDTYQLP LHGQTWLLSG
ELKQDLLLAE INGHKSKIPV SSQGDDFTLF LPSGSYHFKA VQTVVVEEQV SNADKLKAPM
NGTVVTHLVD VGTQVKAGQG LLVMEAMKME YTIEAPFDGI VSEFYFKAGE LVTDGATLLN
VEPLEAVSLA SEPESQTAKE V
//
