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Protein

Linear gramicidin synthase subunit D

Gene

lgrD

Organism
Brevibacillus parabrevis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Activates the 13th to the 16th (Trp, D-Leu, Trp and Gly) amino acids in linear gramicidin and catalyzes the formation of the peptide bond between them. This enzyme is also responsible for the epimerization of the 14th (D-Leu) amino acid. It also catalyzes the NAD(P)H-dependent reduction of the C-terminal glycine residue of the N-formylated 16-mer peptide, that binds to the peptidyl carrier domain of the terminal module of this protein, to form a peptidyl-aldehyde intermediate that is released from the enzyme complex.

Cofactori

pantetheine 4'-phosphateCuratedNote: Binds 4 phosphopantetheines covalently.Curated

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Ligase, Oxidoreductase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

NAD, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Linear gramicidin synthase subunit D
Including the following 5 domains:
ATP-dependent D-leucine adenylase
Short name:
D-LeuA
Alternative name(s):
D-leucine activase
Leucine racemase [ATP-hydrolyzing] (EC:5.1.1.-)
ATP-dependent tryptophan adenylase
Short name:
TrpA
Alternative name(s):
Tryptophan activase
ATP-dependent glycine adenylase
Short name:
GlyA
Alternative name(s):
Glycine activase
Linear gramicidin--PCP reductase (EC:1.-.-.-)
Gene namesi
Name:lgrD
OrganismiBrevibacillus parabrevis
Taxonomic identifieri54914 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaeBrevibacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 50855085Linear gramicidin synthase subunit DPRO_0000193092Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei997 – 9971O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation
Modified residuei2058 – 20581O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation
Modified residuei3579 – 35791O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation
Modified residuei4636 – 46361O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Interactioni

Subunit structurei

Large multienzyme complex composed of 4 subunits; LgrA, LgrB, LgrC and LgrD.

Structurei

3D structure databases

ProteinModelPortaliQ70LM4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini967 – 103468Acyl carrier 1PROSITE-ProRule annotationAdd
BLAST
Domaini2028 – 209467Acyl carrier 2PROSITE-ProRule annotationAdd
BLAST
Domaini3549 – 361668Acyl carrier 3PROSITE-ProRule annotationAdd
BLAST
Domaini4606 – 467368Acyl carrier 4PROSITE-ProRule annotationAdd
BLAST

Domaini

Four module-bearing peptide synthase with a C-terminal epimerization domain. Each module incorporates one amino acid into the peptide product and can be further subdivided into domains responsible for substrate adenylation, thiolation, condensation (not for the initiation module), and epimerization (optional). Contains a reductase domain at the C-terminus.

Sequence similaritiesi

Contains 4 acyl carrier domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di1.10.1200.10. 4 hits.
3.40.50.720. 2 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR013120. Male_sterile_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR010060. NRPS_synth.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR010080. Thioester_reductase-like_dom.
[Graphical view]
PfamiPF00501. AMP-binding. 4 hits.
PF13193. AMP-binding_C. 4 hits.
PF00668. Condensation. 5 hits.
PF07993. NAD_binding_4. 1 hit.
PF00550. PP-binding. 4 hits.
[Graphical view]
SMARTiSM00823. PKS_PP. 4 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 4 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 4 hits.
TIGR01720. NRPS-para261. 1 hit.
TIGR01746. Thioester-redct. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 4 hits.
PS00455. AMP_BINDING. 4 hits.
PS00012. PHOSPHOPANTETHEINE. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q70LM4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNIETYYPV TPLQQGLIFH SLLEPESGAY IVQMGLKLQG PLNIPLFEQA
60 70 80 90 100
WQCLVDRHAI FRTRFVGGKV KEYVQVVLKD LKISLVEHDL IHLSSSEQEA
110 120 130 140 150
FLHHFAKEDR KRGFDIEQAP LMRLNVFHLN SETVHFLWTL HHVLIDGWSM
160 170 180 190 200
PLVFGEVFAA YEMLSKGQPL SLPPVRAYRD YIVWLKKQDL QQAEAFWRTY
210 220 230 240 250
MQGFTEATPL SFGRAYKNPY LDQKQYRELD LTVSEQTSKA LQTLARQHRL
260 270 280 290 300
TVNTIVQGAW ALLLNRYSGQ DDIVFGATVS GRPADLPGVE TMIGLFINTL
310 320 330 340 350
PVRVQVNAEE SVINWLKTLQ QQQADFRQYE YTPLVEIQGW SDVPRGQSLF
360 370 380 390 400
ESILVFENMP VGKSGGGESA ISIVDVYSEE QTNYPFTLVA ASGKTIDIKV
410 420 430 440 450
KFDESQFELA AIERVVDQLH SLLSSIAKNA KQRIGDLSLI SESERQQVLV
460 470 480 490 500
EWNQTAEDYP SGLCIHQAFE QQAEKTPDAV AVAYKNRELT YAQLNERANQ
510 520 530 540 550
LAHRLIRKGV KPDTLVGICL ERSPEMIIGI LGVMKAGAAY VPIDPAHPQE
560 570 580 590 600
RIAYMVADSQ ASALLTQQSL LEILPVTAAH VICLDSDLLA DEPVDNASSE
610 620 630 640 650
VTEQNLAYVI YTSGSTGLPK GVMIEHHSAI NLAYALIDAF DIQPTSRVLQ
660 670 680 690 700
FTSFSFDVSV SEVVMALLAG ATLVIEDRES LLPGPELIQV LQEQRITTVS
710 720 730 740 750
MVSSVLAALP DADLPDLHTL IVGGEAPSRE LVARYAPGRQ FFNCYGPTEA
760 770 780 790 800
TVCSTMMLCQ AGMNNPPIGR PIANATVYVL DANLNPVPVG VPGELYIGGK
810 820 830 840 850
GLARGYWNRP ELTAESFIPH PFGTAGERLY RTGDLVRYRQ DGNLEFLGRI
860 870 880 890 900
DHQVKIRGYR IELGEIENAI RQHPAVQEAV VIAREEKAGD KRLAAYLVAA
910 920 930 940 950
GKAQPPAEEI ALFLKETLPE YMVPAGVVWL DAIPLTVNGK VDRRALPVPD
960 970 980 990 1000
WGQLSTKREY VAPRTPTEEM VANIWSQVLS VERVGSFDDF FELGGHSLLA
1010 1020 1030 1040 1050
TQTVSRLKEA FGVDLPLRVL FECSTVNKLS EWIAAAGEDK SGLSRIPLVP
1060 1070 1080 1090 1100
VSRDRHLPLS FAQQRLWFFD RLMPNSALYN IPTAVRLQGE LDMDALEQSL
1110 1120 1130 1140 1150
QTIIQRHESL RTTFTDHNGE AVSVIHPEID WKLERIDLRE RSEEMRNEAG
1160 1170 1180 1190 1200
LRLAKEEANR PFDLVTGPLM RATIIQTDER DFIFLLNVHH IIADGWSAGI
1210 1220 1230 1240 1250
LIRELFHCYQ AFAKAEAPQL AELPIQYADY AYWQREWLTS DVLDEQLSYW
1260 1270 1280 1290 1300
RAKLGGAEPL LALPTDRPRP AVQSYAGSSI SLLFDDELRA NLLALSKREG
1310 1320 1330 1340 1350
TTLFMTLLAA FQVFLYRYTG QDDILVGTPE AGRSRQETEG LIGFFINTLV
1360 1370 1380 1390 1400
MRTDLSGEPS FKEVLARVRE TALGAYAHQD LPFEKLVDEL NVERSLSYSP
1410 1420 1430 1440 1450
LFQVMFVLQN IPVQADALDG IRILPLEGSQ QVETTKFDLT LTMAEAANGL
1460 1470 1480 1490 1500
AATFEYNTAL FERNTVERMI GHFSSLLKAV AANANQAITA LPLMSEVEEQ
1510 1520 1530 1540 1550
QLVLEWNDTA VAYSTEQLVH ELVAQVARDM PDQPAVVTRD QLLTYGQLEA
1560 1570 1580 1590 1600
KANQLAHYLQ KQGVGRGSLV GICVERSVEM VIGQLAIMKA GAAYIPMDPA
1610 1620 1630 1640 1650
YPKERLAFMM HDASMAIVLT QAKLRQKLPA DTSRLICLDA DWETIAQEPT
1660 1670 1680 1690 1700
AALVNTTAAS DLAYVIYTSG STGTPKGVEI EHAALLNLIF WHQRAYDVTA
1710 1720 1730 1740 1750
TDRASQIAGT AFDASVWEIW PYVTKGATLY LPEEEIRLVP EKLRDWLVAS
1760 1770 1780 1790 1800
NITVSFLPTP LTESMLALEW PGDTALRYML TGGDKLHHYP SEKIPFTLVN
1810 1820 1830 1840 1850
QYGPTENTVV ATAGIVPKEA GQTAAPTIGR PIDNVQVYIL DAHRQPVPVG
1860 1870 1880 1890 1900
VSGELYIGGS SLARGYLNRP DLTQERFVAH PFTEKAGARL YRTGDLVRSL
1910 1920 1930 1940 1950
PDGSIEFIGR ADDQTSIRGF RVELGEVETA IVALPAVKEA VVTVCTDKQG
1960 1970 1980 1990 2000
TKRLAAYLVL EEGAALATGD IRKALKETLP DYMVPAFFTQ LAYLPLTPNG
2010 2020 2030 2040 2050
KVDRKNLPAP DFQRPELEGE FVSPSTEKER RLAAIWKDVL GIEQIGIHDN
2060 2070 2080 2090 2100
FFELGGDSIL SIQIVSRANQ AGLSLAPKQL FEYQTIAELA EIVEEKAAVQ
2110 2120 2130 2140 2150
AEQGAVTGEL PLLPIQKWFF RLPLANRDHW NQSVLLSIQA GIDPAALKQA
2160 2170 2180 2190 2200
VGQLMFQHDA FRMRYTQSES GWLQAMDAPS ETIPFRVEDL SQLAPEEQSS
2210 2220 2230 2240 2250
AIEAIANETQ TQLSLRAGQV VQTIYFHLGK EVPGRLLIVA HHLVVDGVSW
2260 2270 2280 2290 2300
RIILEDLQHA YQQIAAGQEV KLPAKTTSYK EWAQELERYA HSEAFKHEKS
2310 2320 2330 2340 2350
YWLSKSSVHS TELPADMPDS AENTEATVKS VHFSLTVEET KALLQQVPQA
2360 2370 2380 2390 2400
YRTQINDVLL AALAKALGQW TGKRSVFVNV EGHGREELAE HLDLSRTVGW
2410 2420 2430 2440 2450
FTSMYPVHLQ WDETFSVRRA LLTTKEELRA IPNKGLGYGV LRYLHAEQEI
2460 2470 2480 2490 2500
VDAISRIQAD VLFNYMGKID QIVGSDSLFG SAPESSGANL CPSAQRHHLL
2510 2520 2530 2540 2550
DVNSVVAGEQ LHVTWRYSEK LQRESTIAAV AESFMAALRE IVAHCTLPEA
2560 2570 2580 2590 2600
GGYSPSDFPL AVLEQKQIDK HIGFDRQIED VYTLSPLQQG MLFHSLYNQD
2610 2620 2630 2640 2650
SGDYVVQFAV TFQNLDVSVL EKAWQNVLDR HSILRTHFVW EGLSEPHQVV
2660 2670 2680 2690 2700
RKDVKVTLTK EDWRHLQADV QDEMLAAFLE EDRRRSFDIA QAPLSRWVVF
2710 2720 2730 2740 2750
QTKDEEYRFV WSFHHVLLDG WSVPIVLNEL LAHYAAISEG REGKLVPSQP
2760 2770 2780 2790 2800
FSQYIAWLKR QDREKAKPFW TDQLKGFHEP TSLGMGKNVA ASQQKQYKEQ
2810 2820 2830 2840 2850
SVLLSEEATE HLQSFTREHQ LTLNTLVQGA WGWILGSYSG EEEVLFGATG
2860 2870 2880 2890 2900
SGRPADLPGV ETMVGSFINT LPVRVPLQTD ATLLAWLKDL QRRQLEIREY
2910 2920 2930 2940 2950
EYTPLFDIQG WSELPRGSAL FESILVFENY PTVQAAKKGE DEAASATSGV
2960 2970 2980 2990 3000
SLEIHDVAAV EQTNYPLTLV AAPGKQVAFK LKYDQDRFDD AMIERVLNQM
3010 3020 3030 3040 3050
TRLMVYMSKS PELRLNDVAL MDEDERKQVL IDWNRTEKEY PRELCLHHAF
3060 3070 3080 3090 3100
EQQAAKTPEN IALEYKEQSL SYAGLNERAN QLAHLLIAQG VKPDTTVAIC
3110 3120 3130 3140 3150
VERSMEMIIG ILGVLKAGAA YVPIDPAHPE ERIAYMLDDS QAVVVLTQAG
3160 3170 3180 3190 3200
LADKFTQAAA PVICLGEKLF ADRAHVDVDN IQTDVASTNL AYVIYTSGTT
3210 3220 3230 3240 3250
GLPKGVAVEH RSAMNMVQAY IAYFGLDESS RVLQFTSFSF DVSVSEIWQA
3260 3270 3280 3290 3300
LLSGGTLVIE DRESLLPGPD LVRTLRERRI SKVSMASSLL ASLPVAEYPD
3310 3320 3330 3340 3350
LAVLEVGGDA CSRELVARYA TGRKFFNCYG PTEATVGTVI KQLTLDDDTP
3360 3370 3380 3390 3400
TIGRPFPNTK LYVLDQNRKP VPVGVPGELY IGGECLARGY WNRPELTAER
3410 3420 3430 3440 3450
FVANPFGQPG ERLYRTGDLV RYLPDGNVDY LGRFDDQVKI RGYRIELGEI
3460 3470 3480 3490 3500
AEALRQHAAI REAVVLAREV RPGDKRLAAY LTSAAEQELS VDEIKQWLKE
3510 3520 3530 3540 3550
KLPDYMVPAS YTWLPAIPLN VNGKVDRKAL PAPDWGQITA AYVAPRNPLE
3560 3570 3580 3590 3600
EMIANVFAEV LAVEKVGIDD NFFELGGHSL LATQTVSRLR EIVGVELQLR
3610 3620 3630 3640 3650
TLFEHPTVAG LGEQLELLTK QSSRKLAPPI GKVSRKEPLP LSFTQQRLWF
3660 3670 3680 3690 3700
LEQFTQNSSI NNIPSFLRIQ GELDVAAWEA SFSAIILRHE SLRTSFEVRD
3710 3720 3730 3740 3750
GRPVQVIQPH GDWAMTRIDL RALEPAEREA EIKRLAEQAI VQPFDLTKGL
3760 3770 3780 3790 3800
LLRASLVQLD ANDFVFLFVM HHIASDGWSM GILLSELMTN YKAFRQGEAS
3810 3820 3830 3840 3850
PLGELPIQYA DFAVWQREWL SGEVLAEQLG YWREKLKGSE PLLQLPTDRP
3860 3870 3880 3890 3900
RPPVQTYEGE KMSVQFGAEL LKQLQSLSRK EGATLFMTLF AAFQTLLYRY
3910 3920 3930 3940 3950
TNQDDILVGT PIAGRNKQET EQLIGYFINT LVLRTDMSGH PSFRELLARV
3960 3970 3980 3990 4000
RETALEAYAH QDVPFEKLLD ELQLERSMSY SPLFQVMFIL QNIPVQAEPA
4010 4020 4030 4040 4050
GDIQLSSFDL ELGAVTSKFD MTVTMVETPD GLLATLEYNK ALFDSSTITR
4060 4070 4080 4090 4100
MVEHFHKLME EIVANPDQSI TLLPLMREEE EQLLITEWNR TEVPYSREKC
4110 4120 4130 4140 4150
VHEMIEEMVS KAPDSIALIV GEQRVTYGEL NRQANQLAHY LRKQGVGPEV
4160 4170 4180 4190 4200
LVGICAERTV EMMIGLLAIL KAGGAYVPID PAYPAERIAY IIGHSQIPVL
4210 4220 4230 4240 4250
LTQEHLLPTL PEHQAKVICL DRDWATVAVE SEENPGKLAT SDNLIYVIYT
4260 4270 4280 4290 4300
SGSTGNPKGV ALEHRSVIYF LSWAHDTYTP EEMSGVLFST SICFDLSVYE
4310 4320 4330 4340 4350
MFATLTMGGK VIMAENALQL PALPAADQVT LVNTVPSAAT ELVRMKGIPA
4360 4370 4380 4390 4400
SVRVINLCGE PLSNRLAQEL YAFPHVEKVF NLYGPTEDTV YSTHAIVTKG
4410 4420 4430 4440 4450
ATNEPLIGRP QFNTHVFVLD SHRKPVPVGV PGELYLSGSG LARGYLHRPD
4460 4470 4480 4490 4500
LTAERFVQNP FREPGARMYR TGDLVRYLPD GNLQFVGRVD YQVKIRGYRI
4510 4520 4530 4540 4550
ELGEIESVLN RFPGVKEVVL LAREDREGDK CLVAYIVFEA DCTSKIHDLN
4560 4570 4580 4590 4600
HFLADKLPAY MIPQHYMILD SLPKTPNGKL DRKALPKPEY DRSEAGVEYV
4610 4620 4630 4640 4650
APQTPVEIML HAHWAAVLEM ETIGVHDNFF EIGGHSLLAT QLIFKVREEL
4660 4670 4680 4690 4700
QLEVPLRILF ETPTIAGMAK TIEEIIKHGL TSVSQEIDAK GLQDEVALDP
4710 4720 4730 4740 4750
AILAEQPYEG DPSQFQAALL TGATGFLGAF LLRDLLQMTD ADIYCLVRAS
4760 4770 4780 4790 4800
GEEEGLARLR KTLQLYELWD EAQAHRIIPV IGDLAQPRLG LSAGQFDALA
4810 4820 4830 4840 4850
ATVDVIYHNG ALVNFVYPYA ALKKANVIGT EEIIRLAAAK KTKPVHFVST
4860 4870 4880 4890 4900
IFTFASEEGE ESVAVREEDM PENSRILTSG YTQSKWVAEH IVNLARQRGI
4910 4920 4930 4940 4950
PTAIYRCGRM TGDSETGACQ KDDLMWRIAA GIIDLGKAPD MSGDLDMMPV
4960 4970 4980 4990 5000
DFASKGIVHL SMTEHSVNSN FHLLNPNATD YDDLIAAIEN KGFELERVTM
5010 5020 5030 5040 5050
DEWIEAVQED AKDKGMDANS AAPLGNLFSD GHSSRGSVVY VGNKTTRLLR
5060 5070 5080
QADIECPEID EEVFAKVLDY FARTGQLRVT QNTRN
Length:5,085
Mass (Da):567,458
Last modified:July 5, 2004 - v1
Checksum:i8E0618C4AC39BF24
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ566197 Genomic DNA. Translation: CAD92852.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ566197 Genomic DNA. Translation: CAD92852.1.

3D structure databases

ProteinModelPortaliQ70LM4.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.10.1200.10. 4 hits.
3.40.50.720. 2 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR013120. Male_sterile_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR010060. NRPS_synth.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR010080. Thioester_reductase-like_dom.
[Graphical view]
PfamiPF00501. AMP-binding. 4 hits.
PF13193. AMP-binding_C. 4 hits.
PF00668. Condensation. 5 hits.
PF07993. NAD_binding_4. 1 hit.
PF00550. PP-binding. 4 hits.
[Graphical view]
SMARTiSM00823. PKS_PP. 4 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 4 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 4 hits.
TIGR01720. NRPS-para261. 1 hit.
TIGR01746. Thioester-redct. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 4 hits.
PS00455. AMP_BINDING. 4 hits.
PS00012. PHOSPHOPANTETHEINE. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLGRD_BREPA
AccessioniPrimary (citable) accession number: Q70LM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: July 5, 2004
Last modified: September 7, 2016
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Linear gramicidin is a pentadecapeptide antibiotic produced during sporulation.

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.