ID V8NYN0_OPHHA Unreviewed; 1616 AA.
AC V8NYN0;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Branched-chain-amino-acid aminotransferase, mitochondrial {ECO:0000256|ARBA:ARBA00040838};
DE EC=2.6.1.42 {ECO:0000256|ARBA:ARBA00013053};
DE Flags: Fragment;
GN Name=BCAT2 {ECO:0000313|EMBL:ETE66692.1};
GN ORFNames=L345_07520 {ECO:0000313|EMBL:ETE66692.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE66692.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE66692.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE66692.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate +
CC L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42;
CC Evidence={ECO:0000256|ARBA:ARBA00000627};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-
CC glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42;
CC Evidence={ECO:0000256|ARBA:ARBA00000995};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-
CC glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42;
CC Evidence={ECO:0000256|ARBA:ARBA00001745};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU004516};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009320}.
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:ETE66692.1}.
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DR EMBL; AZIM01001503; ETE66692.1; -; Genomic_DNA.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01557; BCAT_beta_family; 1.
DR CDD; cd13248; PH_PEPP1_2_3; 1.
DR Gene3D; 3.30.470.10; -; 1.
DR Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR018300; Aminotrans_IV_CS.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR005786; B_amino_transII.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR InterPro; IPR033939; BCAT_family.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR040392; PKHA4-7_PH.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR11825:SF39; BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11825; SUBGROUP IIII AMINOTRANSFERASE; 1.
DR Pfam; PF13561; adh_short_C2; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00081; GDHRDH.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:ETE66692.1};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004516};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ETE66692.1};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 55..154
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 178..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 444..478
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 188..204
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE66692.1"
SQ SEQUENCE 1616 AA; 178660 MW; 94B4B9CF2205B9E5 CRC64;
MSEGDRPKSG LSLASSTATI SSVSMGTKPH VARPVRKVHT FGKRANSIKR DPNSPVIMRG
WLYKQDSSGL KLWKRRWFVL SNYCLFYYRD SREEMVLGSI LLPSYEIRTA FSKEKKNRRF
VFKAEHPGMR TYYFSADTQL DMNSWIRAMN QSAAAECNCG NLSLSSQTHG CPSPISCTKF
SSRPRTPLPP SSESPPPPSP SQISQPSPVF SLRSSRAYSL PVAPAESPKL PQAHPSDMHD
AHWSPHDAHR SPHDAHRSPH DAHRSPPRSV VAQAASCDDL SIMSSPRTLH ANIPMGRVDI
APNKCLPNNP YAVVSPAHKG HSLTPADRYD VFPTSEDSYA RRYAQSPHLH RVRPVGEDGL
VPSIGRPQQN RFTDRGYLSP SVGPSRALVM SRLHGRLITP HSASSSYLHL PPLPPLPTRS
TPGKRTSVGI TALLTKLCGQ DKVLRGLEEE TGQLRIEKER LEKALEVTHL RMEEFKGQDA
TVEKICYQQR QLQDELVHTR ARLCDLALDS ERVWEDYTAL ENDVQMLKGS LEHIRTSGHP
QDQAAAQQDL WRIHDILAGL RCSPANYRTL ENRRSGVSPS SPPPLDSNLG ANHHPLLSCT
ETEESTPSCR PETGKQARMG SKQQDVPGSA NWQQSPSTSS RGQLGASQHV DGLKGSPNHS
YIEPPESGKG KLGRGADSIR PVTSPNPLFF PHVQVASSET TVPRRSRMSA QEQLDRMQRN
QEAKRKSEAA QPSPLGHWRD SPKHGSSRPL PNAPPEPSPK EGMQFGEVKP PRCPPTPEWE
RQRVIQLSYA LATEASQRGK LLTGRTSSCS SLDDLLASED GLNHHYFPGD GTCIKLDSSN
TTAGHNQKIT QSPSCSTDSK VANQVPTSPQ ATKPMFSASE ASDWSLPCPC EESWLPSKLK
TPQPTSHLFD PAREEPFLLS SAHWEEPLPQ PTNWNACFCR TANWVLPPVW DLEMWAADQK
LVTNPSLNNG RCVHWRVHHG AKVVFCAPAS EEEKGKGLER ELAEGGGSGE GCFVACDVLC
EADMKFALPY LRKTKGNIIN VASIVAHFGQ KLAVPYVATK GAVVAMTKAM AIDESQYGVR
VNSISPSNIW TPGWEKLASQ AASAEAIIKE GKDAQASALW ENGNFMGRMG TPAECAKAAL
YLASDATSPT PKVASQPGNL PTPLKTASGI GQMRRRQRRT EGADPSGLVS RRPRPVPLNH
SLNNSMAVTM GVPGCLRQVL RGKAADVLLF APQRFFSTTF KASDLQIELN KHLKPKPDSS
KLVFGKNFTD HMLTVEWSKE NGWGKPHIKP FQNLSLHPAS SALHYSVELF EGMKAFRGSD
QRIRLFRPML NMDRMLQSSL RACLPDKQQE CRVLVFLQAF DQSELLECIQ QLIRVDQDWV
PHSSTASLYI RPILIGTEPS LGVSVANHAL LFVILGPVGP YFTTGSFNPV SLLADPRFVR
AWMGGEICDK VTLESNYGPT IYVQGEAAKL GCQQVLWLYG DDHQITEVGT MNIFLFWKDQ
EGDMELVTPP LNGIILPGVT RQSLLDLARK WGEFKVSERL VTMSELIKGL EEKRVKEIFG
SGTACVVCPV DRILYQGKNY HIPTMENGPE IAKRFLKELT DIQYGRISSD WAQEVC
//
