ID K7GHN2_PELSI Unreviewed; 694 AA.
AC K7GHN2;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Methylcrotonoyl-CoA carboxylase 1 {ECO:0000313|Ensembl:ENSPSIP00000019793.1};
GN Name=MCCC1 {ECO:0000313|Ensembl:ENSPSIP00000019793.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000019793.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000019793.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; AGCU01198554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01198555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01198556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K7GHN2; -.
DR STRING; 13735.ENSPSIP00000019793; -.
DR Ensembl; ENSPSIT00000019886.1; ENSPSIP00000019793.1; ENSPSIG00000017510.1.
DR eggNOG; KOG0238; Eukaryota.
DR GeneTree; ENSGT00940000156941; -.
DR HOGENOM; CLU_000395_3_1_1; -.
DR OMA; FINKPKH; -.
DR TreeFam; TF105650; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0002169; C:3-methylcrotonyl-CoA carboxylase complex, mitochondrial; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
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:Ensembl.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.40; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; 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};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000007267}.
FT DOMAIN 20..466
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 139..336
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 598..687
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 694 AA; 77157 MW; E1EEFCD6577922E7 CRC64;
RKWIWGQRCL KFASTIERRN IEKVLIANRG EIACRVMRTA RKMGLKSVAV YSDADKNSMH
VAMADEAYFI GPAASQQSYL AMEKIIQVAK MSTAQAIHPG YGFLSENTEF AELCKQEGII
FIGPPSSAIR DMGIKSTSKA IMSAAGVPII EGYHGEDQSD KCLKEHARRI GYPVMIKAVR
GGGGKGMRIA HSEKDFLDQL ESARREAKKS FNDDAVLIEK FVDNPRHVEV QVFGDQHGNA
VYLFERDCSV QRRHQKIIEE APGPGIEPEV RRKLGEAAVK AAKAVNYVGA GTVEFIMDSQ
HNFYFMEMNT RLQVEHPVTE MITGTDLVEW QLRVAAGEKI PLMQEEIALS GHAFEARIYA
EDPNNNFMPG AGPLLHLSTP PPDRFTRIET GVRQGDEVSV HYDPMIAKLV VWAEDRQSAL
KKLRYSLHQY NIVGLSTNIE FLLSLSGHPQ FEAGNVHTNF ISQHHDELFP VKQATPNEVL
CQAVLGLLLR ERMMTDAFRV KSYDKFSPFA SSSGRRINMS YTRKLTLLDG ENKVDISIDY
NQDGSYNMQI KDKAFNVSGN ISNENDSTYL RCSVNGIVYK SKVVILDNTI CLFSLKGSAQ
IGLPVPKYLS ETSATGPQGG AVAPMTGTIE KVFVKAGDKV QAGDPLMVMI AMKMEHTIRA
PKAGIIKKVN YQEGSQANRH ASLVELVDED MESE
//
