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Protein

Tyrocidine synthase 1

Gene

tycA

Organism
Brevibacillus parabrevis
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

In the first step of peptide synthesis this enzyme activates phenylalanine and racemizes it to the D-isomer.

Miscellaneous

Tyrocidine is a mixture of four cyclic decapeptides, tyrocidine A (D-Phe-Pro-Phe-D-Phe-Asn-Gln-Tyr-Val-Orn-Leu), B, C, and D, in which Phe, at positions 3, 4, and Tyr residues are gradually replaced by Trp, depending on the relative concentrations of these amino acids in the growth medium.

Catalytic activityi

ATP + L-phenylalanine + H2O = AMP + diphosphate + D-phenylalanine.

Cofactori

pantetheine 4'-phosphateCuratedNote: Binds 1 phosphopantetheine covalently.Curated

Pathwayi: tyrocidine biosynthesis

This protein is involved in the pathway tyrocidine biosynthesis, which is part of Antibiotic biosynthesis.
View all proteins of this organism that are known to be involved in the pathway tyrocidine biosynthesis and in Antibiotic biosynthesis.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase, Ligase, Multifunctional enzyme
Biological processAntibiotic biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00180

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrocidine synthase 1
Alternative name(s):
Tyrocidine synthase I
Including the following 2 domains:
ATP-dependent D-phenylalanine adenylase
Short name:
D-PheA
Alternative name(s):
D-phenylalanine activase
Phenylalanine racemase [ATP-hydrolyzing] (EC:5.1.1.11)
Gene namesi
Name:tycA
OrganismiBrevibacillus parabrevis
Taxonomic identifieri54914 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaeBrevibacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001930931 – 1088Tyrocidine synthase 1Add BLAST1088

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei563O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Interactioni

Subunit structurei

Large multienzyme complex of TycA, TycB and TycC.

Structurei

Secondary structure

11088
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi29 – 39Combined sources11
Beta strandi43 – 48Combined sources6
Beta strandi51 – 54Combined sources4
Helixi55 – 72Combined sources18
Beta strandi79 – 82Combined sources4
Helixi88 – 100Combined sources13
Beta strandi103 – 106Combined sources4
Helixi113 – 123Combined sources11
Beta strandi126 – 130Combined sources5
Helixi132 – 140Combined sources9
Beta strandi145 – 149Combined sources5
Helixi150 – 152Combined sources3
Beta strandi171 – 178Combined sources8
Beta strandi186 – 191Combined sources6
Helixi192 – 205Combined sources14
Beta strandi213 – 216Combined sources4
Helixi224 – 233Combined sources10
Turni234 – 236Combined sources3
Beta strandi238 – 241Combined sources4
Helixi244 – 248Combined sources5
Helixi250 – 259Combined sources10
Beta strandi264 – 267Combined sources4
Helixi269 – 272Combined sources4
Helixi277 – 279Combined sources3
Beta strandi284 – 291Combined sources8
Helixi295 – 301Combined sources7
Turni302 – 304Combined sources3
Beta strandi305 – 311Combined sources7
Beta strandi321 – 324Combined sources4
Beta strandi338 – 340Combined sources3
Beta strandi344 – 349Combined sources6
Beta strandi362 – 368Combined sources7
Helixi379 – 385Combined sources7
Beta strandi386 – 388Combined sources3
Beta strandi390 – 392Combined sources3
Beta strandi395 – 406Combined sources12
Beta strandi412 – 417Combined sources6

3D structure databases

ProteinModelPortaliP09095
SMRiP09095
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini528 – 602CarrierPROSITE-ProRule annotationAdd BLAST75

Domaini

One-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), and N methylation (optional).

Sequence similaritiesi

Family and domain databases

Gene3Di1.10.1200.10, 1 hit
3.30.559.10, 1 hit
InterProiView protein in InterPro
IPR010071 AA_adenyl_domain
IPR036736 ACP-like_sf
IPR025110 AMP-bd_C
IPR020459 AMP-binding
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
IPR023213 CAT-like_dom_sf
IPR001242 Condensatn
IPR010060 NRPS_synth
IPR009081 PP-bd_ACP
IPR006162 Ppantetheine_attach_site
PfamiView protein in Pfam
PF00501 AMP-binding, 1 hit
PF13193 AMP-binding_C, 1 hit
PF00668 Condensation, 1 hit
PF00550 PP-binding, 1 hit
PRINTSiPR00154 AMPBINDING
SUPFAMiSSF47336 SSF47336, 1 hit
TIGRFAMsiTIGR01733 AA-adenyl-dom, 1 hit
TIGR01720 NRPS-para261, 1 hit
PROSITEiView protein in PROSITE
PS00455 AMP_BINDING, 1 hit
PS50075 CARRIER, 1 hit
PS00012 PHOSPHOPANTETHEINE, 1 hit

Sequencei

Sequence statusi: Complete.

P09095-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLANQANLID NKRELEQHAL VPYAQGKSIH QLFEEQAEAF PDRVAIVFEN
60 70 80 90 100
RRLSYQELNR KANQLARALL EKGVQTDSIV GVMMEKSIEN VIAILAVLKA
110 120 130 140 150
GGAYVPIDIE YPRDRIQYIL QDSQTKIVLT QKSVSQLVHD VGYSGEVVVL
160 170 180 190 200
DEEQLDARET ANLHQPSKPT DLAYVIYTSG TTGKPKGTML EHKGIANLQS
210 220 230 240 250
FFQNSFGVTE QDRIGLFASM SFDASVWEMF MALLSGASLY ILSKQTIHDF
260 270 280 290 300
AAFEHYLSEN ELTIITLPPT YLTHLTPERI TSLRIMITAG SASSAPLVNK
310 320 330 340 350
WKDKLRYINA YGPTETSICA TIWEAPSNQL SVQSVPIGKP IQNTHIYIVN
360 370 380 390 400
EDLQLLPTGS EGELCIGGVG LARGYWNRPD LTAEKFVDNP FVPGEKMYRT
410 420 430 440 450
GDLAKWLTDG TIEFLGRIDH QVKIRGHRIE LGEIESVLLA HEHITEAVVI
460 470 480 490 500
AREDQHAGQY LCAYYISQQE ATPAQLRDYA AQKLPAYMLP SYFVKLDKMP
510 520 530 540 550
LTPNDKIDRK ALPEPDLTAN QSQAAYHPPR TETESILVSI WQNVLGIEKI
560 570 580 590 600
GIRDNFYSLG GDSIQAIQVV ARLHSYQLKL ETKDLLNYPT IEQVALFVKS
610 620 630 640 650
TTRKSDQGII AGNVPLTPIQ KWFFGKNFTN TGHWNQSSVL YRPEGFDPKV
660 670 680 690 700
IQSVMDKIIE HHDALRMVYQ HENGNVVQHN RGLGGQLYDF FSYNLTAQPD
710 720 730 740 750
VQQAIEAETQ RLHSSMNLQE GPLVKVALFQ TLHGDHLFLA IHHLVVDGIS
760 770 780 790 800
WRILFEDLAT GYAQALAGQA ISLPEKTDSF QSWSQWLQEY ANEADLLSEI
810 820 830 840 850
PYWESLESQA KNVSLPKDYE VTDCKQKSVR NMRIRLHPEE TEQLLKHANQ
860 870 880 890 900
AYQTEINDLL LAALGLAFAE WSKLAQIVIH LEGHGREDII EQANVARTVG
910 920 930 940 950
WFTSQYPVLL DLKQTAPLSD YIKLTKENMR KIPRKGIGYD ILKHVTLPEN
960 970 980 990 1000
RGSLSFRVQP EVTFNYLGQF DADMRTELFT RSPYSGGNTL GADGKNNLSP
1010 1020 1030 1040 1050
ESEVYTALNI TGLIEGGELV LTFSYSSEQY REESIQQLSQ SYQKHLLAII
1060 1070 1080
AHCTEKKEVE RTPSDFSVKG LQMEEMDDIF ELLANTLR
Length:1,088
Mass (Da):122,672
Last modified:July 15, 1999 - v2
Checksum:i6AC4804199572027
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti197 – 242NLQSF…SLYIL → ICNPFSKIRLASPSKTGSGF LPACRSTHPFGKCSWLCCLA PRVHP in CAA31623 (PubMed:3267240).CuratedAdd BLAST46
Sequence conflicti359 – 360GS → AD in CAA31623 (PubMed:3267240).Curated2
Sequence conflicti496L → I AA sequence (PubMed:8193142).Curated1
Sequence conflicti665L → V in CAA31623 (PubMed:3267240).Curated1
Sequence conflicti737L → F in CAA31623 (PubMed:3267240).Curated1
Sequence conflicti756 – 790EDLAT…WLQEY → KIWQPDTRRHLQGKRSVCPK KRILFKAGHNGCKNN in CAA31623 (PubMed:3267240).CuratedAdd BLAST35
Sequence conflicti876 – 894QIVIH…IEQAN → KSSFIWRGTGARTSSNRQT in CAA31623 (PubMed:3267240).CuratedAdd BLAST19

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13237 Genomic DNA Translation: CAA31623.1
AF004835 Genomic DNA Translation: AAC45928.1
M16442 mRNA Translation: AAA22876.1 Frameshift.
PIRiA26878
T31074 YGBSTB

Similar proteinsi

Entry informationi

Entry nameiTYCA_BREPA
AccessioniPrimary (citable) accession number: P09095
Secondary accession number(s): O30407
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 15, 1999
Last modified: March 28, 2018
This is version 115 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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