ID G5EGD0_CAEEL Unreviewed; 3393 AA.
AC G5EGD0;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase {ECO:0000256|ARBA:ARBA00039053};
DE EC=4.4.1.14 {ECO:0000256|ARBA:ARBA00039053};
GN ORFNames=CELE_T04F3.1 {ECO:0000313|EMBL:CCA65609.1}, T04F3.1
GN {ECO:0000313|EMBL:CCA65609.1, ECO:0000313|WormBase:T04F3.1b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCA65609.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCA65609.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCA65609.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-
CC methionine; ethylene from S-adenosyl-L-methionine: step 1/2.
CC {ECO:0000256|ARBA:ARBA00037888}.
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DR EMBL; BX284605; CCA65609.1; -; Genomic_DNA.
DR RefSeq; NP_001256364.1; NM_001269435.1.
DR SMR; G5EGD0; -.
DR EPD; G5EGD0; -.
DR PeptideAtlas; G5EGD0; -.
DR EnsemblMetazoa; T04F3.1b.1; T04F3.1b.1; WBGene00011436.
DR GeneID; 179608; -.
DR AGR; WB:WBGene00011436; -.
DR WormBase; T04F3.1b; CE45986; WBGene00011436; -.
DR GeneTree; ENSGT00940000175293; -.
DR HOGENOM; CLU_224868_0_0_1; -.
DR OrthoDB; 1328656at2759; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00011436; Expressed in larva and 3 other cell types or tissues.
DR ExpressionAtlas; G5EGD0; baseline and differential.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0006520; P:amino acid metabolic process; IBA:GO_Central.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43795:SF10; AMINOTRAN_1_2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43795; BIFUNCTIONAL ASPARTATE AMINOTRANSFERASE AND GLUTAMATE/ASPARTATE-PREPHENATE AMINOTRANSFERASE-RELATED; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00753; ACCSYNTHASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 1: Evidence at protein level;
KW Aminotransferase {ECO:0000313|EMBL:CCA65609.1};
KW Proteomics identification {ECO:0007829|EPD:G5EGD0,
KW ECO:0007829|PeptideAtlas:G5EGD0};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Transferase {ECO:0000313|EMBL:CCA65609.1}.
FT DOMAIN 3040..3377
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 110..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1303..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1469..1525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1666..1722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1769..1795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1832..1857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2030..2100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2157..2186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2319..2340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..689
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1035
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1506..1520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1678..1709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2032..2046
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2047..2061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2064..2100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2166..2186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3393 AA; 385022 MW; E7135C38ED619FB9 CRC64;
MPRRREKFVE ITKTVTVTEI VNGAPDKHPS SCEVKVTNVS PAGPHPVNVS IKHLHEKWHS
CEELDRSDNG EDLGKGTVIR IQETHKPFNC TQKKHQTNKF VYEDVINTKM ESSTKSRQPP
SANSTLFNRS SDNIIDLEFR HPILRETSEK KSERTEQKAN GNNGTRRRFA DLRKRVSTTT
KTSVTETENV TTTRRSSSAH STHSKRSSAK PEVHTLYYRK FVDEETKGAD DDSSDSGSVI
IYRDAVTRRS RSADPLQNSS PTMSPIAPPR KRLGREESLH YYRDDDEVIQ EQSSTEKSRR
VTVKSPEPGN TSVSMNDNVE GRNLTAGITS ISMNDSCTDT SYESRFSTIP RARSSPPGNH
RVNHIQVNVI GPIRVSEPES RHPVVGSVGE DVTMDIYIER RRSGSNPRRD SHVSFETLEA
PPKPPRRSKY DEHIRIGDPI ATSTPMTTIE RKQTREERVS TESGQSSRKS TRSSRPPDIN
IIECETFLKE TRSPARTPAT PIVVINQTPS SRRSSQDLLG EPGQRRRKST VTDIDWYAAF
NMKDPSSPTK IARPSFASHN EERKASRDLR RRASDSSMIG IPPADIDLNQ IFLCTVPPEI
KKDEKCQCNA CRLIRMSEAE RAVRIERSGR SRQSRSFTRT TEFETRSSTL PSRHRTAPVD
IELEDIFNPK PFSHPSANSK PPTPPNRRRH PPSASVAHSQ SSFVDESPSQ HFVTTTIDRN
QVTPVTTTTT NMRESGPLLH ENSHNQLLSS SDNWVAQMMN DASEWENNVS SRKSSILSTS
STSARKASVA RRISVDELTK PEKRKSRQAV PLPPSDVSID DIFTALTPRK EEVQSERKTF
IVTRKQRAQD VDAIDFEKDR ETPIAPPRSG KRKSDATENQ PEITLELDVE KHEIDSSKVS
TSTINLNDES METRNTNDSK DSFDDEVNPR NQRLVVEIPF SEPRVTSTAT IQLESSDVAG
ENSENKRPVI SMRSKSEIAK KEKDAQRSGF VIIPHSKEHI LDESNISMDD VFNTTPHDQC
RVPDIDADSS KHTSSDSREV STVTINLDNV FPTEEPKLVA KDNCEIEAEE ERIGKRIKQF
ERTTGEQEIS KNSEPTEDEM PDEKDHRTSA VSIDLDKVFV QGTAKKPEND EFDEKIKRGI
AEFERSKQEK EVQRSGVAET SHSGKHIFDE SNISMDDVFN TSQKYKSDEK LSTPERTVEP
EVSTATMNLD NIISASGIAT REENTNVLEE EERIQKRVEE FKKTTENLEI QKEVVLTKEE
VDNSDVKEHR TSAVNIDLEK VFIHGSSKKP KNDDEKIRRG IAEFERTKQE KEAQRSTVIE
TSQSNSRIFE ESSISMDDVF NNSLHNESQV SEITEASDPS DLVLTSTTFH NVIEEKIDDD
VTKTDSNVEE EKEQVRLRID EFKRPTEEQN LQKEFELTKK EEEYSVKMEN RTSAVSIDLD
KVFDQSSKET TVSNETDEKI KRGIAEFERS KQEKEVQRSG VAETSHSGKH IFDESNISMD
DVFNTSQKYK SDEKLSSPER TVEPEVSTAT MNLDNIIFAS GIATREENTD VLEEEERIQK
RVEEFKKTTE NLEIQKEVVL TKEEVDNSDV KEHRTSAVNI DLDDVFIQRS SKHPENDEDD
EKIRRGIAEF ERTKQEKEAQ RSAVIETSQS NKHIFDKSNI SMDEVFNESQ NGQKDSSNID
MKETDMPEKE RDDQRYVDVH RDKKPFENGE FEPTFNGSKI SNEPKQISIT TINLDNVFPT
EEPKLVAEDN CEIEAEEERI RKRIKQFERT TGEQEILKNS EPAEDETSDE KKHRTAAVSI
DLDKVFVQGT AKKPENDEFD EKIKRGIAEF ERSKQEKEVQ RSGVAETSHS SKHIFDESNI
SMDDVFNTSQ KYKSDEKLST PERTVEPEVS TATMNLDNII FASGIATREK NTDVLEEEER
IQKRVEEFKK TTENLEIQKE VVLTKEEGDN SDVKDHKASA VNIDLDDVFI QRSSKHPEND
EDDEKIRRGI AEFERTKQEK EAQRSTVIET QYSSKDMFNE SDISLDVVFN TSQKDKSDEK
LSSPERTVEP EVSTATVNLD NMVALSKERR KENNETQEEE EQIQKRVEEF KESTEEQKIQ
KSIELTKEEC TSDEKELKTY SGSIDLDKVF IQGSSKKPRN DESDERINRG IAEFERTKQE
KEAQRSVVVE TSPSNKHISD ESSISMDEIF SRSQDNKSTS NFEKSGSIPI IVLPGEEKEV
ASASINLNGV FLEGKQKTST DYGREKVNKV QENSGSYSTR HAMDGASISL DDIFNTSSTS
QKTETDKIDN SQEFPQLSKP VLKSSISLDD LFNNTSGIEK TTSEKTTTTT TTRTETTTDT
YSKRSTSTLV DRFGYETATP PAISIAAISF DQPSSSSPQA FPRSKHQNLS SLTVPGKWNE
SMMSNTSTIS LDDSFNNSFS KSNTSQVYEP RMRKPLTLPV DNWIDNLVSE ATNEATKEAP
KTPKSDTLNY FRSPTRISQE IKYEWVADMI GDIDRKNKGG HQSEEEHLQK HDSTWVSSVV
YRPTLETSAY TLRSSQLNTD CKMEIDLENV FDECLMGKKK DDEHCECSAC RLTEQELEEI
KKRKIELENM TSEQKIIISE PSDRRKSVDF SNPSQISLNE VFSPEVPLRI ETEHAPAPST
SSPPLESTRI YYLSPKVSET VTTTHQWKDA GIPMDEIFSP VSSTADGNRR FSNFYEDRSG
WDTIGSEDSG VMSGGDRGRR RSTRITDQVI DEAFQGIFDS QPSTSTAHPK PVRTETHYDD
YYITSLQQED LDATDSEVDG ENLDVSTFVD DILGKSMDEA AFLSSTKSLR EHTDTSIDRK
KSGEKVHSYY RNRTDTSIDK RSKPEVITED LETSELQDEI MKLVFVEPSV SKSDSSANIK
ASQNKSTTKP CDEELLEIEI KSEYFLIKGS YSLLIPKSDP LGKMLQKLRE QNDSLATLDF
SLTRKLKKLL VNCIREKAGS LDMVSMSSQY EGLSSRGQSL IESIDHASAT FLKMNVDKYE
PTRNPNGVVN FCTAENNICT PLLEDRFKHL ELFFPNIEHL VRYPPAGGWP ETRRVLVKYF
KEFMGAGVTI DELVLTASTR TGYDVTSYCL FEQDDILLTN GPIYTGTISN VQEKAQCQVV
CVETDLSNPR LDVKMYEAEL NRQIALENTV SGVIIVNPHN PLGVTFPPEQ VISLCNWASS
KNLRVVIDEV FANSVFDKLN SKFRPFLSYR HRLHRPDSVA WLWSVSKDFG LPGLKFAVIH
TTNEGLCQAA TKLQMYYPCS PFVQDFAVNL LSDSEWLREF HREVNKRISI HYRYTSDNLK
RLEIPFIPAQ AGIFVFADFS KHLTSLDSVG ELALFERLAE AGVMLTPGVH QKCHVFGWFR
IVFACTKEEL EEGFRRLYIH LGSQLQPVGT VEY
//
