P26046 (ACVS2_PENCH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase
EC=6.3.2.26

Alternative name(s):
Delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase
Short name=ACV synthetase
Short name=ACVS

Gene names

Name:

PCBAB

Organism

Penicillium chrysogenum (Penicillium notatum)

Taxonomic identifier

5076 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Penicillium › Penicillium chrysogenum complex

Protein attributes

Sequence length	3791 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Each of the constituent amino acids of the tripeptide acv are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates.
Catalytic activity	L-2-aminohexanedioate + L-cysteine + L-valine + 3 ATP + H2O = N-(L-5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + 3 AMP + 3 diphosphate.
Cofactor	Binds 3 phosphopantetheines covalently.
Pathway	Antibiotic biosynthesis; penicillin G biosynthesis; penicillin G from L-alpha-aminoadipate and L-cysteine and L-valine: step 1/3.
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family. Contains 3 acyl carrier domains.

Ontologies

Keywords
Biological process	Antibiotic biosynthesis
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding Phosphopantetheine
Molecular function	Ligase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	antibiotic biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase activity Inferred from electronic annotation. Source: EC acyl carrier activity Inferred from electronic annotation. Source: InterPro cofactor binding Inferred from electronic annotation. Source: InterPro hydrolase activity, acting on ester bonds Inferred from electronic annotation. Source: InterPro phosphopantetheine binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 3791	3791	N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase		PRO_0000193061
Regions
	Domain	853 – 924	72	Acyl carrier 1
	Domain	1939 – 2008	70	Acyl carrier 2
	Domain	3028 – 3095	68	Acyl carrier 3
	Region	307 – 1068	762	Domain 1 (adipate-activating)
	Region	1392 – 2157	766	Domain 2 (cysteine-activating)
	Region	2574 – 3242	669	Domain 3 (valine-activating)
Sites
	Active site	3631	1	For thioesterase activity By similarity
Amino acid modifications
	Modified residue	885	1	O-(pantetheine 4'-phosphoryl)serine By similarity
	Modified residue	1971	1	O-(pantetheine 4'-phosphoryl)serine By similarity
	Modified residue	3058	1	O-(pantetheine 4'-phosphoryl)serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P26046 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 1B628000F8A00492	FASTA	3,791	425,922
	10 20 30 40 50 60 MTQLKPPNGT TPIGFSATTS LNASGSSSVK NGTIKPSNGI FKPSTRDTMD PCSGNAADGS 70 80 90 100 110 120 IRVRFRGGIE RWKECVNQVP ERCDLSGLTT DSTRYQLAST GFGDASAAYQ ERLMTVPVDV 130 140 150 160 170 180 HAALQELCLE RRVSVGSVIN FSVHQMLKGF GNGTHTITAS LHREQNLQNS SPSWVVSPTI 190 200 210 220 230 240 VTHENRDGWS VAQAVESIEA GRGSEKESVT AIDSGSSLVK MGLFDLLVSF VDADDARIPC 250 260 270 280 290 300 FDFPLAVIVR ECDANLSLTL RFSDCLFNEE TICNFTDALN ILLAEAVIGR VTPVADIELL 310 320 330 340 350 360 SAEQKQQLEE WNNTDGEYPS SKRLHHLIEE VVERHEDKIA VVCDERELTY GELNAQGNSL 370 380 390 400 410 420 ARYLRSIGIL PEQLVALFLD KSEKLIVTIL GVWKSGAAYV PIDPTYPDER VRFVLDDTKA 430 440 450 460 470 480 RAIIASNQHV ERLQREVIGD RNLCIIRLEP LLASLAQDSS KFPAHNLDDL PLTSQQLAYV 490 500 510 520 530 540 TYTSGTTGFP KGIFKQHTNV VNSITDLSAR YGVAGQHHEA ILLFSACVFE PFVRQTLMAL 550 560 570 580 590 600 VNGHLLAVIN DVEKYDADTL LPFIRRHSIT YLNGTASVLQ EYDFSDCPSL NRIILVGENL 610 620 630 640 650 660 TEARYLALRQ RFKNRILNEY GFTESAFVTA LKIFDPESTR KDTSLGRPVR NVKCYILNPS 670 680 690 700 710 720 LKRVPIGATG ELHIGGLGIS KGYLNRPELT PHRFIPNPFQ TDCEKQLGIN SLMYKTGDLA 730 740 750 760 770 780 RWLPNGEVEY LGRADFQIKL RGIRIEPGEI ETMLAMYPRV RTSLVVSKKL RNGPEETTNE 790 800 810 820 830 840 HLVGYYVCDS ASVSEADLLS FLEKKLPRYM IPTRLVQLSQ IPVNVNGKAD LRALPAVDIS 850 860 870 880 890 900 NSTEVRSDLR GDTEIALGEI WADVLGARQR SVSRNDNFFR LGGHSITCIQ LIARIRQRQR 910 920 930 940 950 960 LSVSISVEDV FATRTLERMA DLLQNKQQEK CDKPHEAPTE LLEENAATDN IYLANSLQQG 970 980 990 1000 1010 1020 FVYHYLKSME QSDAYVMQSV LRYNTTLSPD LFQRAWKHAQ QSFPALRLRF SWEKEVFQLL 1030 1040 1050 1060 1070 1080 DQDPPLDWRF LYFTDVAAGA VEDRKLEDLR RQDLTERFKL DVGRLFRVYL IKHSENRFTC 1090 1100 1110 1120 1130 1140 LFSCHHAILD GWSLPLLFEK VHETYLQLLH GDNLTSSMDD PYTRTQRYLH AHREDHLDFW 1150 1160 1170 1180 1190 1200 AGVVQKINER CDMNALLNER SRYKVQLADY DQVQEQRQLT IALSGDAWLA DLRQTCSAQG 1210 1220 1230 1240 1250 1260 ITLHSILQFV WHAVLHAYGG GTHTITGTTI SGRNLPILGI ERAVGPYINT LPLVLDHSTF 1270 1280 1290 1300 1310 1320 KDKTIMEAIE DVQAKVNVMN SRGNVELGRL HKTDLKHGLF DSLFVLENYP NLDKSRTLEH 1330 1340 1350 1360 1370 1380 QTELGYSIEG GTEKLNYPLA VIAREVETTG GFTVSICYAS ELFEEVMISE LLHMVQDTLM 1390 1400 1410 1420 1430 1440 QVARGLNEPV GSLEYLSSIQ LEQLAAWNAT EAEFPDTTLH EMFENEASQK PDKIAVVYEE 1450 1460 1470 1480 1490 1500 TSLTYRELNE RANRMAHQLR SDVSPNPNEV IALVMDKSEH MIVNILAVWK SGGAYVPIDP 1510 1520 1530 1540 1550 1560 GYPNDRIQYI LEDTQALAVI ADSCYLPRIK GMAASGTLLY PSVLPANPDS KWSVSNPSPL 1570 1580 1590 1600 1610 1620 SRSTDLAYII YTSGTTGRPK GVTVEHHGVV NLQVSLSKVF GLRDTDDEVI LSFSNYVFDH 1630 1640 1650 1660 1670 1680 FVEQMTDAIL NGQTLLVLND GMRGDKERLY RYIEKNRVTY LSGTPSVVSM YEFSRFKDHL 1690 1700 1710 1720 1730 1740 RRVDCVGEAF SEPVFDKIRE TFHGLVINGY GPTEVSITTH KRLYPFPERR MDKSIGQQVH 1750 1760 1770 1780 1790 1800 NSTSYVLNED MKRTPIGAVG ELYLGGEGVV RGYHNRADVT AERFIPNPFQ SEEDKREGRN 1810 1820 1830 1840 1850 1860 SRLYKTGDLV RWIPGSSGEV EYLGRNDFQV KIRGLRIELG EIEAILSSYH GIKQSVVIAK 1870 1880 1890 1900 1910 1920 DCREGAQKFL VGYYVADAAL PSAAIRRFMQ SRLPGYMVPS RLILVSKFPV TPSGKLDTKA 1930 1940 1950 1960 1970 1980 LPPAEEESEI DVVPPRSEIE RSLCDIWAEL LEMHPEEIGI YSDFFSLGGD SLKSTKLSFM 1990 2000 2010 2020 2030 2040 IHESFNRAVS VSALFCHRTV EAQTHLILND AADVHEITPI DCNDTQMIPV SRAQERLLFI 2050 2060 2070 2080 2090 2100 HEFENGSNAY NIDAAFELPG SVDASLLEQA LRGNLARHEA LRTLLVKDHA TGIYLQKVLS 2110 2120 2130 2140 2150 2160 PDEAQGMFSV NVDTAKQVER LDQEIASLSQ HVFRLDDELP WEARILKLES GGLYLILAFH 2170 2180 2190 2200 2210 2220 HTCFDAWSLK VFEQELRALY AALQKTKSAA NLPALKAQYK EYALYHRRQL SGDRMRNLSD 2230 2240 2250 2260 2270 2280 FWLRKLIGLE PLQLITDRPR PVQFKYDGDD LSIELSKKET ENLRGVAKRC KSSLYVVLVS 2290 2300 2310 2320 2330 2340 VYCVMLASYA NQSDVSVGIP VSHRTHPQFQ SVIGFFVNLV VLRVDISQSA ICGLIRRVMK 2350 2360 2370 2380 2390 2400 ELVDAQLHQD MPFQEVTKLL QVDNDPSRHP LVQNVFNFES RANGEHDARS EDEGSLAFNQ 2410 2420 2430 2440 2450 2460 YRPVQPVDSV AKFDLNATVT ELESGLRVNF NYATSLFNKS TIQGFLHTYE YLLRQLSELS 2470 2480 2490 2500 2510 2520 AEGINEDTQL SLVRPTENGD LHLPLAQSPL ATTAEEQKVA SLNQAFEREA FLAAEKIAVV 2530 2540 2550 2560 2570 2580 QGDRALSYAD LNGQANQLAR YIQSVSCIGA DDGIALMLEK SIDTIICILA IWKAGAAYVP 2590 2600 2610 2620 2630 2640 LDPTYPPGRV QLILEEIKAK AVLVHSSHAS KCERHGAKVI AVDSPAIETA VSQQSAADLP 2650 2660 2670 2680 2690 2700 TIASLGNLAY IIFTSGTSGK PKGVLVEQKA VLLLRDALRE RYFGRDCTKH HGVLFLSNYV 2710 2720 2730 2740 2750 2760 FDFSVEQLVL SVLSGHKLIV PPAEFVADDE FYRMASTHGL SYLSGTPSLL QKIDLARLDH 2770 2780 2790 2800 2810 2820 LQVVTAAGEE LHATQYEKMR RRFNGPIYNA YGVTETTVYN IIAEFTTNSI FENALREVLP 2830 2840 2850 2860 2870 2880 GTRAYVLNAA LQPVPFDAVG ELYLAGDSVT RGYLNQPLLT DQRFIPNPFC KEEDIAMGRF 2890 2900 2910 2920 2930 2940 ARLYKTGDLV RSRFNRQQQP QLEYLGRGDL QIKMRGYRIE ISEVQNVLTS SPGVREGAVV 2950 2960 2970 2980 2990 3000 AKYENNDTYS RTAHSLVGYY TTDNETVSEA DILTFMKARL PTYMVPSHLC CLEGALPVTI 3010 3020 3030 3040 3050 3060 NGKLDVRRLP EIINDSAQSS YSPPRNIIEA KMCRLWESAL GMERCGIDDD LFKLGGDSIT 3070 3080 3090 3100 3110 3120 SLHLVAQIHN QVGCKITVRD IFEHRTARAL HDHVFMKDSD RSNVTQFRTE QGPVIGEAPL 3130 3140 3150 3160 3170 3180 LPIQDWFLSK ALQHPMYWNH TFYVRTPELD VDSLSAAVRD LQQYHDVFRM RLKREEVGFV 3190 3200 3210 3220 3230 3240 QSFAEDFSPA QLRVLNVKDV DGSAAVNEIL DGWQSGFNLE NGPIGSIGYL HGYEDRSARV 3250 3260 3270 3280 3290 3300 WFSVHHMAID TVSWQILVRD LQTLYRNGSL GSKGSSFRQW AEAIQNYKAS DSERNHWNKL 3310 3320 3330 3340 3350 3360 VMETASSISA LPTSTGSRVR LSRSLSPEKT ASLIQGGIDR QDVSVYDSLL TSVGLALQHI 3370 3380 3390 3400 3410 3420 APTGPSMVTI EGHGREEVDQ TLDVSRTMGW FTTMYPFEIP RLSTENIVQG VVAVSERFRQ 3430 3440 3450 3460 3470 3480 VPARGVGYGT LYGYTQHPLP QVTVNYLGQL ARKQSKPKEW VLAVGDNEFE YGLMTSPEDK 3490 3500 3510 3520 3530 3540 DRSSSAVDVT AVCIDGTMII DVDSAWSLEE SEQFISSIEE GLNKILDGRA SQQTSRFPDV 3550 3560 3570 3580 3590 3600 PQPAETYTPY FEYLEPPRQG PTLFLLPPGE GGAESYFNNI VKRLRQTNMV VFNNYYLHSK 3610 3620 3630 3640 3650 3660 RLRTFEELAE MYLDQVRGIQ PHGPYHFIGW SFGGILAMEM SRRLVASDEK IGFLGIIDTY 3670 3680 3690 3700 3710 3720 FNVRGATRTI GLGDTEILDP IHHIYNPDPA NFQRLPSATD RIVLFKAMRP NNKYESENQR 3730 3740 3750 3760 3770 3780 RLYEYYDALD STDWTACYQA IPTSSWSRLR TIHTFPGSEI HNRWSRCVRL SRNTSLAIDP 3790 SLAAQYIGRW K

References

[1]

"The cluster of penicillin biosynthetic genes. Identification and characterization of the pcbAB gene encoding the alpha-aminoadipyl-cysteinyl-valine synthetase and linkage to the pcbC and penDE genes." Diez B., Gutierrez S., Barredo J.L., van Solingen P., van der Voort L.H.M., Martin J.F. J. Biol. Chem. 265:16358-16365(1990) [PubMed: 2129535] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: AS-P-78.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M57425 Genomic DNA. Translation: AAA63415.1.
PIR	YGPLV8. A37886.
3D structure databases
ProteinModelPortal	P26046.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR010071. AA_adenyl_domain. IPR009081. Acyl_carrier_prot-like. IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. IPR001242. Condensatn. IPR006163. Phsphopanteth-bd. IPR006162. PPantetheine_attach_site. IPR001031. Thioesterase. [Graphical view]
Gene3D	G3DSA:1.10.1200.10. ACP_like. 3 hits.
Pfam	PF00501. AMP-binding. 3 hits. PF00668. Condensation. 3 hits. PF00550. PP-binding. 3 hits. PF00975. Thioesterase. 1 hit. [Graphical view]
SUPFAM	SSF47336. ACP_like. 3 hits.
TIGRFAMs	TIGR01733. AA-adenyl-dom. 3 hits.
PROSITE	PS50075. ACP_DOMAIN. 3 hits. PS00455. AMP_BINDING. 3 hits. PS00012. PHOSPHOPANTETHEINE. 3 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACVS2_PENCH

Accession

Primary (citable) accession number: P26046

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	September 21, 2011
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program