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Database: UniProt
Entry: P27743
LinkDB: P27743
Original site: P27743 
ID   ACVS_AMYLA              Reviewed;        3649 AA.
AC   P27743;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-OCT-2017, entry version 96.
DE   RecName: Full=N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase;
DE            EC=6.3.2.26;
DE   AltName: Full=Delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase;
DE            Short=ACV synthetase;
DE            Short=ACVS;
GN   Name=pcbAB;
OS   Amycolatopsis lactamdurans (Nocardia lactamdurans).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis.
OX   NCBI_TaxID=1913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VAR LC 411;
RX   PubMed=1956290; DOI=10.1111/j.1365-2958.1991.tb01885.x;
RA   Coque J.J.R., Martin J.F., Calzada J.G., Liras P.;
RT   "The cephamycin biosynthetic genes pcbAB, encoding a large multidomain
RT   peptide synthetase, and pcbC of Nocardia lactamdurans are clustered
RT   together in an organization different from the same genes in
RT   Acremonium chrysogenum and Penicillium chrysogenum.";
RL   Mol. Microbiol. 5:1125-1133(1991).
CC   -!- FUNCTION: Each of the constituent amino acids of the tripeptide
CC       acv are activated as aminoacyl-adenylates with peptide bonds
CC       formed through the participation of amino acid thioester
CC       intermediates.
CC   -!- CATALYTIC ACTIVITY: L-2-aminohexanedioate + L-cysteine + L-valine
CC       + 3 ATP + H(2)O = N-(L-5-amino-5-carboxypentanoyl)-L-cysteinyl-D-
CC       valine + 3 AMP + 3 diphosphate.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC       Note=Binds 3 phosphopantetheines covalently.;
CC   -!- PATHWAY: Antibiotic biosynthesis; penicillin G biosynthesis;
CC       penicillin G from L-alpha-aminoadipate and L-cysteine and L-
CC       valine: step 1/3.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. {ECO:0000305}.
DR   EMBL; X57310; CAA40561.1; -; Genomic_DNA.
DR   PIR; S18268; S18268.
DR   ProteinModelPortal; P27743; -.
DR   SMR; P27743; -.
DR   ESTHER; nocla-acvs; Thioesterase.
DR   UniPathway; UPA00149; UER00239.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0050564; F:N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1200.10; -; 3.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
DR   Pfam; PF00501; AMP-binding; 3.
DR   Pfam; PF13193; AMP-binding_C; 3.
DR   Pfam; PF00668; Condensation; 3.
DR   Pfam; PF00550; PP-binding; 3.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00823; PKS_PP; 3.
DR   SUPFAM; SSF47336; SSF47336; 3.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 3.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 3.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; ATP-binding; Ligase; Multifunctional enzyme;
KW   Nucleotide-binding; Phosphopantetheine; Phosphoprotein; Repeat.
FT   CHAIN         1   3649       N-(5-amino-5-carboxypentanoyl)-L-
FT                                cysteinyl-D-valine synthase.
FT                                /FTId=PRO_0000193059.
FT   DOMAIN      783    860       Carrier 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00258}.
FT   DOMAIN     1859   1936       Carrier 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00258}.
FT   DOMAIN     2909   2984       Carrier 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00258}.
FT   REGION      401    861       Domain 1 (adipate-activating).
FT   REGION     1014   1937       Domain 2 (cysteine-activating).
FT   REGION     2079   2985       Domain 3 (valine-activating).
FT   ACT_SITE   3502   3502       For thioesterase activity. {ECO:0000250}.
FT   MOD_RES     820    820       O-(pantetheine 4'-phosphoryl)serine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00258}.
FT   MOD_RES    1896   1896       O-(pantetheine 4'-phosphoryl)serine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00258}.
FT   MOD_RES    2944   2944       O-(pantetheine 4'-phosphoryl)serine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00258}.
SQ   SEQUENCE   3649 AA;  404088 MW;  6FD095704F858E6B CRC64;
     MTSARHLKSA ADWCARIDAI AGQRCDLEML LKDEWRHRVA VRDSDTAVRA TQEKELTISG
     QDYTALKQAL GAMPLEAFAL ATLHSVLHAY GHGHQTVVAF LRDGKVLPVV VDHLEQAGLT
     CAEAAEQLED AVAREDMYLP PEELLQRGLF DALLVLADGH LGFTELPPAP LVTIVRDDPA
     AGCLHWRIAY AGEFFEDKII AGVLDVAREV LGQFIGRPEQ LVADIDLVSA EQELQLHQWN
     GTDGEFDEDK RLNELFEDVV RRAPDREAVV CGDVRLTYRE VNERANQFAH WLIQGPVRVR
     PGALIGLYLD KSDLGVVATF GIWKSGAAYV PIDPAYPAER IRFLVGDTGL SGIVTNRRHA
     ERLREVLGDE HASVHVIEVE AVVAGPHPEQ ARENPGLALS SRDRAYVTYT SGTTGVPKGV
     PKYHYSVVNS ITDLSERYDM RRPGTERVAL FASYVFEPHL RQTLIALINE QTLVIVPDDV
     RLDPDLFPEY IERHGVTYLN ATGSVLQHFD LRRCASLKRL LLVGEELTAS GLRQLREKFA
     GRVVNEYAFT EAAFVTAVKE FGPGVTERRD RSIGRPLRNV KWYVLSQGLK QLPIGAIGEL
     YIGGCGVAPG YLNRDDLTAE RFTANPFQTE EEKARGRNGR LYRTGDLARV LLNGEVEFMG
     RADFQLKLNG VRVEPGEIEA QATEFPGVKK CVVVAKENAT GDRHLVGYYL VEDGAEVAEA
     DLIAFLEQRL IRIMVPARMV RLTSIPVNVN GKVDWRALPD VSLHPAPANA MNGALLAIDG
     SNAPLLAITE QLRAIWSEVL GVPQNRIGER DDFFRLGGQS ISCILLIARV RQRLSLSLGV
     EDVFALRTLD ALAGHLESQG HAEPEVVAEE VTTGSEPVRV LANGLQQGLL YHHLKTAGGD
     DAYVVQSVHR YHAPIRPELM KDAWQAARQT YPALRLRFDW AEEPVQIVDN DDKPFDWRFV
     DLSATADDAE QEARVRELQE RDRTEPYDLA GGRLFRVYLI KQREDLFSLI FSCHHIILDG
     WSLPVLHDEV HRNYLALRAG QPIESDVDNA YVAAQRYWEA HRNDHAAYWV EQLGRIDERG
     DFAGLLNEKS RYRVSLGDYD HVQRHRTRKL YLGADLTGAL KAGCAADQVT LHSVLQFVWH
     KVLHAIGGGN TTVVGTIVSG RNLPVDGIEN SAGLFINTLP LIVDHDQQAG QNVAEAVRDI
     QAAVNTMNSK SIVELGRLQS GEMKRRLFDT LLVLENYPRL LDEEEELAHQ EALRFEKAYD
     ADKVDYPIAV VAREEGDELT VTLWYAGELF DEDTIDTLLD VARTLFRQVT EDIARPVREL
     DLISPSMRAR FDSWNETAEE FPADKTLHAV FEEMAERWPD EIAVVYRENR LTYRELNERA
     NRLAHYLRSV VELRPDDLVA LVLDKSELMI TAIIAAWKTG AAYVPIDSGY PDDRISFMLS
     DTAARVVVTN EIHSDRLRSL AETGTPVLEI ELLHLDDQPA VNPVTETTST DLAYAIYTSG
     TTGKPKAVLV EHRGVVNLQV SLAKLFGLDK AHRDEALLSF SNYIFDHFVE QMTDALLNGQ
     KLVVLDDSMR TDPGRLCRYM NDEQVTYLSG TPSVLSLYDY SSATSLTRID AIGEDFTEPV
     FAKIRGTFPG LIINGYGPTE ISITSHKRPY PPDVHRVNKS IGFPVANTKC HVLNKAMKPV
     PVGGIGELYI GGIGVTRGYL NREDLTADRF VENPFQTAEE RRLGENGRLY KTGDLVRWLP
     NGEVEYLGRT DLQVKIRGQR VELGEVEAAL SSYPGVVRSL VVAREHAVGQ KYLVGFYVGE
     QEFDEQDLKQ WMRKKLPESV VPARVLRITD IPVTPSGKLD ARRLPETDFG AGEGAEYVAP
     VSEFELKLCG IWAQVLEIAP DRIGVHDDFF ALGGDSIRAM ALAQAITTGF GQGLGVATVL
     QHTTLAAQAE HIQAAALEHT AWTPPPTAVE HPPVSLAQER LLFIDDFEGG TAAYNIPFVL
     RLPAHTRAAL PGALGTLVRR HPALRTLLKT DDQGVRRQYP IPADDVRLEV PSTTVDSRAE
     LDEVLTERAG YVFRLHEELP IRAEAFDHGD EIYLSVVVHH SCFDGWSWDI FRRELAALLD
     GVPEADLGAL RGTYGEFAVW QRQYLTGKRL AALTEFWTGA LGGFETIALP LDHPRPPRFD
     YRGRELEFEL DERTTEALRE LARTARVSLY SVLLGAWCLM LNMYTGQHDL VVGTPSANRG
     RPEFDRAVGF FANLLALRVR VDPAATLPAY VRSVGEAVVA AQVHGELPFE QLVKELKVEK
     DPSRHPILQL NFTLQNVSDH TSALTGYQPD SGGWTTTKFD LSATMTETAT GLAGNLTYAA
     SLFDDTSASG FIATFKHVLA EFASAAAQTP IAQLTALDEP GQAALPDATR RARRPGGPGR
     CTRLFEEVAA TWPDRVAVVH GDVRLTYREL NERANRLAHH LRSVAEPRAD ELIALVLDKS
     ELTLVAILAV WKAGAAYMPI DPSYPDDRIA FMLSDTGAKL VLAGEAHGSR VRGLTSGDVL
     DLEQLDLTGE PAENPVTETT STELAYAIYT SGTTGKPKAV LVSHGSVDSF RAQLSGRYFG
     SPDESAEAVL FLANYVFDFS VEQLALSVLG GHKLLVPPPS AADDPAFYEL ANREGLSYLS
     GTPTQVERFD LARLSHLRCV LVAGEAFQPQ HFEKMRGEFA GPILNAYGTT ETTVYNTVHR
     FEPGDAYRNT LGAPLGNTRL YVLGDGMKLL PTGAVGELYL AGDCVTEGYL HRPELTRERF
     LPNPFAAESG RFPMIYRTGD VVRRGPDGEL QYLGRNDAQV KINGLRIEPG EVEAALAGCS
     GVRQCAVVAG ADPQAPERKR LVGYYLPEPG AAVDEADLFA ALRAQLMPSM VPSLLVRLDR
     PLPMTITGKL DVDALPSADF SPKRAAYAAP RDRVEARLCH LWSAQLPGGT VGIDDDFFRC
     GGDSISALHL ASQVQREIER KVSVKYLFDH PTVRSFVDNV LSGLAESSGD DEPEQGRLTG
     ECPMLPIQEW FFAKPLADRH RWNHNFAIRT PPLDPGELRT ALDRLVEHHD AFRLRFPESG
     GEVYAEDAAP ITLHELDVRG LADADLRQRL VDWQRTFDLA NGPTACAAYL HGFDDGTARV
     WFALHHLVVD TVSWHILAQD LEILYNGGDL GAKTGSYRQW AQAVRDYTPA EGEREFWAET
     TRDMESAELL AQTEGTTRRR EEFALTAPDT RTLLAESPWA YDTEVNDLLL TATGFALRSI
     TRQATNHLTV EGHGRELFEG APDVRDTVGW FTTMHPFAVE VDPGDLGRSV LATRANRRRV
     PHHGIGYGAL FGGEAPLPAV SFNYLGRLGE GDGQPTEAWQ LDPALSGSHT VDGNRLANRS
     SIDVTMSCTG GRLVAVVDSL LGEAATRLFA SELKVWLERL VSHTATVARN EPAREATTEL
     FDPYILVNED AERTLFVLPP GEGGAESYLS NLARQLPDLR LVLFNNVHLH TPMGSFEELG
     RYYVEHIRRL QPSGPYHLLG WSFGGVLSLE ISRQLARAGE RIDDLLLIDP YFGMRQASAN
     IGLPGVEDIL DPINYHYRPD EADLARLAGR LGNLVLFKAG EPNDVVNGPH QPRLFEYYHG
     TRFNHLDLLL PAAAIEVCDL AGETHHSWVR NEKLVRLMCE RISTSLGSD
//
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