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Database: UniProt
Entry: A0KVT3_SHESA
LinkDB: A0KVT3_SHESA
Original site: A0KVT3_SHESA 
ID   A0KVT3_SHESA            Unreviewed;       674 AA.
AC   A0KVT3;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   24-JAN-2024, entry version 93.
DE   SubName: Full=3-methylcrotonoyl-CoA carboxylase, alpha subunit {ECO:0000313|EMBL:ABK47902.1};
DE            EC=6.4.1.4 {ECO:0000313|EMBL:ABK47902.1};
GN   OrderedLocusNames=Shewana3_1669 {ECO:0000313|EMBL:ABK47902.1};
OS   Shewanella sp. (strain ANA-3).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=94122 {ECO:0000313|EMBL:ABK47902.1, ECO:0000313|Proteomes:UP000002589};
RN   [1] {ECO:0000313|Proteomes:UP000002589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANA-3 {ECO:0000313|Proteomes:UP000002589};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA   Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; CP000469; ABK47902.1; -; Genomic_DNA.
DR   RefSeq; WP_011716699.1; NC_008577.1.
DR   AlphaFoldDB; A0KVT3; -.
DR   STRING; 94122.Shewana3_1669; -.
DR   KEGG; shn:Shewana3_1669; -.
DR   eggNOG; COG4770; Bacteria.
DR   HOGENOM; CLU_000395_3_1_6; -.
DR   OMA; LVKWQLM; -.
DR   OrthoDB; 9763189at2; -.
DR   Proteomes; UP000002589; Chromosome.
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:ABK47902.1};
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          589..666
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   674 AA;  73521 MW;  545D05C9FEDB83D6 CRC64;
     MLTKLLIANR GEIACRIIKT AQAMGVRTVA LYSDADKNAR HVAMADESFY LGGSAPADSY
     LKGDLIIEIA KKAQAQAIHP GYGFLSENAD FARKCEAAGI VFVGPGSDAI DAMGSKSAAK
     AIMTAAQVPL VPGYHGDDQT DATLKAEALK IGFPMLIKAA YGGGGKGMRI VEHEGEIMDA
     INSARREAAS SFGNDKLLME RYLRQPRHVE VQVFADTFGN AIYLSDRDCS IQRRHQKVVE
     EAPAPGLSDE LRTQMGEAAV AAAKAIDYVG AGTVEFLLDT DNSFYFMEMN TRLQVEHPVT
     EMVTGQDLVK WQLMVASGQP LPLKQDEVRI HGHAFEVRIY AEDPQNEFLP ASGKLNFLRE
     PEQSKYVRID SGIRENDVIS NFYDPMIAKL IVWDESRPRA LQRLVHALES YQISGLKHNI
     EFLANIAEHP AFAKADFSTD FINRYGDALI SSASSETDTA LAFAALYQVL ARKEAAKAQA
     INSADPYSPW GQVSGFRLNS VSQHSIALLD DAHELQQLVL LDFGDHYQLS QPTADGQVSK
     SLSGELKQDL LLAEINGHKS KVPVSAQGDD FTLFLPSGSY HFRAVKTQVV EAESSNEDKL
     KAPMNGTVVT HLVEVGAEVN AGQGLLVMEA MKMEYTIEAP FDGIVTEFYF KAGELVSDGA
     VLLHVEPKAQ SEEA
//
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