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Protein

Arginine deiminase

Gene

arcA

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

Functioni

Catalytic activityi

L-arginine + H2O = L-citrulline + NH3.

Pathwayi: L-arginine degradation via ADI pathway

This protein is involved in step 1 of the subpathway that synthesizes carbamoyl phosphate from L-arginine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Arginine deiminase (arcA), Arginine deiminase (arcA), Arginine deiminase (arcA)
  2. no protein annotated in this organism
This subpathway is part of the pathway L-arginine degradation via ADI pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes carbamoyl phosphate from L-arginine, the pathway L-arginine degradation via ADI pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei398 – 3981Amidino-cysteine intermediateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Arginine metabolism

Enzyme and pathway databases

BRENDAi3.5.3.6. 3521.
SABIO-RKP23793.
UniPathwayiUPA00254; UER00364.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine deiminase (EC:3.5.3.6)
Short name:
ADI
Alternative name(s):
Arginine dihydrolase
Short name:
AD
Gene namesi
Name:arcA
OrganismiMycoplasma arginini
Taxonomic identifieri2094 [NCBI]
Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 410409Arginine deiminasePRO_0000182219Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
410
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 183Combined sources
Beta strandi20 – 256Combined sources
Helixi30 – 345Combined sources
Helixi37 – 393Combined sources
Helixi40 – 434Combined sources
Helixi51 – 6616Combined sources
Turni67 – 693Combined sources
Beta strandi71 – 744Combined sources
Helixi75 – 8511Combined sources
Helixi88 – 10013Combined sources
Helixi108 – 11912Combined sources
Helixi124 – 13310Combined sources
Helixi137 – 1404Combined sources
Beta strandi145 – 1506Combined sources
Helixi154 – 1574Combined sources
Beta strandi161 – 1677Combined sources
Beta strandi169 – 1724Combined sources
Helixi178 – 1814Combined sources
Helixi184 – 19310Combined sources
Turni195 – 1995Combined sources
Beta strandi202 – 2043Combined sources
Helixi206 – 2083Combined sources
Helixi214 – 2163Combined sources
Beta strandi217 – 2193Combined sources
Beta strandi221 – 23212Combined sources
Helixi235 – 24713Combined sources
Beta strandi255 – 2606Combined sources
Helixi270 – 2723Combined sources
Beta strandi274 – 2763Combined sources
Beta strandi278 – 2847Combined sources
Helixi286 – 2883Combined sources
Turni289 – 2913Combined sources
Beta strandi293 – 2986Combined sources
Turni299 – 3013Combined sources
Beta strandi309 – 3113Combined sources
Helixi315 – 3239Combined sources
Beta strandi328 – 3314Combined sources
Helixi339 – 3479Combined sources
Turni348 – 3514Combined sources
Beta strandi354 – 3574Combined sources
Beta strandi360 – 3645Combined sources
Helixi368 – 3769Combined sources
Beta strandi380 – 3845Combined sources
Helixi387 – 3904Combined sources
Turni396 – 3994Combined sources
Beta strandi401 – 4055Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LXYX-ray2.00A/B2-410[»]
1S9RX-ray1.60A/B1-410[»]
ProteinModelPortaliP23793.
SMRiP23793. Positions 2-410.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23793.

Family & Domainsi

Sequence similaritiesi

Belongs to the arginine deiminase family.Curated

Family and domain databases

HAMAPiMF_00242. Arg_deiminase. 1 hit.
InterProiIPR003876. Arg_deiminase.
IPR033199. DDAH/AD.
[Graphical view]
PANTHERiPTHR12737. PTHR12737. 3 hits.
PIRSFiPIRSF006356. Arg_deiminase. 1 hit.
PRINTSiPR01466. ARGDEIMINASE.
TIGRFAMsiTIGR01078. arcA. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23793-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVFDSKFKG IHVYSEIGEL ESVLVHEPGR EIDYITPARL DELLFSAILE
60 70 80 90 100
SHDARKEHKQ FVAELKANDI NVVELIDLVA ETYDLASQEA KDKLIEEFLE
110 120 130 140 150
DSEPVLSEEH KVVVRNFLKA KKTSRELVEI MMAGITKYDL GIEADHELIV
160 170 180 190 200
DPMPNLYFTR DPFASVGNGV TIHYMRYKVR QRETLFSRFV FSNHPKLINT
210 220 230 240 250
PWYYDPSLKL SIEGGDVFIY NNDTLVVGVS ERTDLQTVTL LAKNIVANKE
260 270 280 290 300
CEFKRIVAIN VPKWTNLMHL DTWLTMLDKD KFLYSPIAND VFKFWDYDLV
310 320 330 340 350
NGGAEPQPVE NGLPLEGLLQ SIINKKPVLI PIAGEGASQM EIERETHFDG
360 370 380 390 400
TNYLAIRPGV VIGYSRNEKT NAALEAAGIK VLPFHGNQLS LGMGNARCMS
410
MPLSRKDVKW
Length:410
Mass (Da):46,507
Last modified:January 23, 2007 - v4
Checksum:iE15C9A8AC90176FA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761I → T in CAA36693 (PubMed:2325633).Curated
Sequence conflicti120 – 1201A → S in CAA36693 (PubMed:2325633).Curated
Sequence conflicti126 – 1261E → K in CAA38210 (PubMed:2228248).Curated
Sequence conflicti375 – 41036EAAGI…KDVKW → DKKDYLRPISI in CAA36693 (PubMed:2325633).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54141 Genomic DNA. Translation: CAA38080.1.
X54312 Genomic DNA. Translation: CAA38210.1.
X52459 Genomic DNA. Translation: CAA36693.2.
PIRiA41465.
RefSeqiWP_004416214.1. NZ_AP014657.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54141 Genomic DNA. Translation: CAA38080.1.
X54312 Genomic DNA. Translation: CAA38210.1.
X52459 Genomic DNA. Translation: CAA36693.2.
PIRiA41465.
RefSeqiWP_004416214.1. NZ_AP014657.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LXYX-ray2.00A/B2-410[»]
1S9RX-ray1.60A/B1-410[»]
ProteinModelPortaliP23793.
SMRiP23793. Positions 2-410.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00254; UER00364.
BRENDAi3.5.3.6. 3521.
SABIO-RKP23793.

Miscellaneous databases

EvolutionaryTraceiP23793.

Family and domain databases

HAMAPiMF_00242. Arg_deiminase. 1 hit.
InterProiIPR003876. Arg_deiminase.
IPR033199. DDAH/AD.
[Graphical view]
PANTHERiPTHR12737. PTHR12737. 3 hits.
PIRSFiPIRSF006356. Arg_deiminase. 1 hit.
PRINTSiPR01466. ARGDEIMINASE.
TIGRFAMsiTIGR01078. arcA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiARCA_MYCAR
AccessioniPrimary (citable) accession number: P23793
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 101 of the entry and version 4 of the sequence. [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

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.