(data stored in ACNUC7421 zone)

SWISSPROT: C6WDR2_ACTMD

ID   C6WDR2_ACTMD            Unreviewed;       415 AA.
AC   C6WDR2;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 57.
DE   RecName: Full=Arginine deiminase {ECO:0000256|HAMAP-Rule:MF_00242};
DE            Short=ADI {ECO:0000256|HAMAP-Rule:MF_00242};
DE            EC=3.5.3.6 {ECO:0000256|HAMAP-Rule:MF_00242};
DE   AltName: Full=Arginine dihydrolase {ECO:0000256|HAMAP-Rule:MF_00242};
DE            Short=AD {ECO:0000256|HAMAP-Rule:MF_00242};
GN   Name=arcA {ECO:0000256|HAMAP-Rule:MF_00242};
GN   OrderedLocusNames=Amir_0083 {ECO:0000313|EMBL:ACU34057.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34057.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34057.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
CC   -!- CATALYTIC ACTIVITY: L-arginine + H(2)O = L-citrulline + NH(3).
CC       {ECO:0000256|HAMAP-Rule:MF_00242, ECO:0000256|SAAS:SAAS00533843}.
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC       pathway; carbamoyl phosphate from L-arginine: step 1/2.
CC       {ECO:0000256|HAMAP-Rule:MF_00242, ECO:0000256|SAAS:SAAS00533834}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00242,
CC       ECO:0000256|SAAS:SAAS00533837}.
CC   -!- SIMILARITY: Belongs to the arginine deiminase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00242, ECO:0000256|SAAS:SAAS00533823}.
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DR   EMBL; CP001630; ACU34057.1; -; Genomic_DNA.
DR   ProteinModelPortal; C6WDR2; -.
DR   STRING; 446462.Amir_0083; -.
DR   EnsemblBacteria; ACU34057; ACU34057; Amir_0083.
DR   KEGG; ami:Amir_0083; -.
DR   eggNOG; ENOG4105CEU; Bacteria.
DR   eggNOG; COG2235; LUCA.
DR   HOGENOM; HOG000284536; -.
DR   KO; K01478; -.
DR   OMA; QERATMH; -.
DR   OrthoDB; POG091H06H4; -.
DR   UniPathway; UPA00254; UER00364.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016990; F:arginine deiminase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00242; Arg_deiminase; 1.
DR   InterPro; IPR003876; Arg_deiminase.
DR   InterPro; IPR033199; DDAH/AD.
DR   PANTHER; PTHR12737; PTHR12737; 1.
DR   PIRSF; PIRSF006356; Arg_deiminase; 1.
DR   PRINTS; PR01466; ARGDEIMINASE.
PE   3: Inferred from homology;
DR   PRODOM; C6WDR2.
DR   SWISS-2DPAGE; C6WDR2.
KW   Arginine metabolism {ECO:0000256|HAMAP-Rule:MF_00242,
KW   ECO:0000256|SAAS:SAAS00533855};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00242,
KW   ECO:0000256|SAAS:SAAS00533821};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00242,
KW   ECO:0000256|SAAS:SAAS00533854, ECO:0000313|EMBL:ACU34057.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213}.
FT   ACT_SITE    404    404       Amidino-cysteine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00242,
FT                                ECO:0000256|PIRSR:PIRSR006356-1}.
SQ   SEQUENCE   415 AA;  44216 MW;  E09238E7E0190410 CRC64;
     MTAHIEHTQS ATPAPGPAPR VDSEVGPLRT VLLHRPGAEL KRLTPRNNDQ LLFDGVPWVD
     RAQEEHDAFA GVLRSRGVEV LLLGDELVRA LHDDRARIAG VHSAVDERRL GIHLADALRS
     HLSGLAPEAL ATILTSGMTF EELPAAEGAS LVRRMHQPGD FAVDPLPNLL FTRDSSVWVG
     DRVAITSLAM PARGRETALT DLIYAYHPRF AKTGRAYGAH SAPLEGGDVL LLAPGVLAIG
     VGERTTPAGA ESFARSALAD GLAHTVLAVP IAQQRATMHL DTVCTMVDRD AVVMYPAVRD
     NLFAYPVRQD GSGGVRVSGP SPFLEAAAEA MGIDRLRVID TGLDAVTAER EQWDDGNNTL
     AVGPGLVVAY ERNVETNARL EEAGVEVLRI SGSELGSGRG GPRCMSCPID RAPLV
//

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