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Database: UniProt/TrEMBL
Entry: E1UN63_BACAS
LinkDB: E1UN63_BACAS
Original site: E1UN63_BACAS 
ID   E1UN63_BACAS            Unreviewed;       458 AA.
AC   E1UN63;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   26-NOV-2014, entry version 27.
DE   RecName: Full=Argininosuccinate lyase {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000256|SAAS:SAAS00067294};
DE            Short=ASAL {ECO:0000256|HAMAP-Rule:MF_00006};
DE            EC=4.3.2.1 {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000256|SAAS:SAAS00067347};
DE   AltName: Full=Arginosuccinase {ECO:0000256|HAMAP-Rule:MF_00006};
GN   Name=argH {ECO:0000256|HAMAP-Rule:MF_00006,
GN   ECO:0000313|EMBL:CBI43862.1};
GN   OrderedLocusNames=BAMF_2736 {ECO:0000313|EMBL:CBI43862.1};
OS   Bacillus amyloliquefaciens (strain ATCC 23350 / DSM 7 / BCRC 11601 /
OS   NBRC 15535 / NRRL B-14393).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=692420 {ECO:0000313|EMBL:CBI43862.1, ECO:0000313|Proteomes:UP000006562};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM7;
RX   DOI=10.1099/ijs.0.023267-0 ;
RA   Borriss R., Chen X., Rueckert C., Blom J., Becker A., Baumgarth B.,
RA   Fan B., Pukall R., Schumann P., Sproer C., Junge H., Vater J.,
RA   Puhler A., Klenk H.P.;
RT   "Relationship of Bacillus amyloliquefaciens clades associated with
RT   strains DSM7T and FZB42: a proposal for Bacillus amyloliquefaciens
RT   subsp. amyloliquefaciens subsp. nov. and Bacillus amyloliquefaciens
RT   subsp. plantarum subsp. nov. based on their discriminating complete
RT   genome sequences.";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2010).
RN   [2] {ECO:0000313|Proteomes:UP000006562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23350 / DSM 7 / BCRC 11601 / NBRC 15535 / NRRL B-14393
RC   {ECO:0000313|Proteomes:UP000006562};
RX   PubMed=21262282; DOI=10.1016/j.jbiotec.2011.01.006;
RA   Ruckert C., Blom J., Chen X., Reva O., Borriss R.;
RT   "Genome sequence of B. amyloliquefaciens type strain DSM7(T) reveals
RT   differences to plant-associated B. amyloliquefaciens FZB42.";
RL   J. Biotechnol. 155:78-85(2011).
CC   -!- CATALYTIC ACTIVITY: 2-(N(omega)-L-arginino)succinate = fumarate +
CC       L-arginine. {ECO:0000256|HAMAP-Rule:MF_00006,
CC       ECO:0000256|SAAS:SAAS00067374}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       arginine from L-ornithine and carbamoyl phosphate: step 3/3.
CC       {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000256|SAAS:SAAS00067273}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006,
CC       ECO:0000256|SAAS:SAAS00067213}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00006}.
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DR   EMBL; FN597644; CBI43862.1; -; Genomic_DNA.
DR   RefSeq; YP_003921332.1; NC_014551.1.
DR   ProteinModelPortal; E1UN63; -.
DR   EnsemblBacteria; CBI43862; CBI43862; BAMF_2736.
DR   GeneID; 9781576; -.
DR   KEGG; bao:BAMF_2736; -.
DR   PATRIC; 42474730; VBIBacAmy172706_2939.
DR   HOGENOM; HOG000242744; -.
DR   KO; K01755; -.
DR   BioCyc; BAMY692420:GHU2-2828-MONOMER; -.
DR   UniPathway; UPA00068; UER00114.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR   Gene3D; 1.10.275.10; -; 1.
DR   HAMAP; MF_00006; Arg_succ_lyase; 1.
DR   InterPro; IPR029419; Arg_succ_lyase_C.
DR   InterPro; IPR009049; Argininosuccinate_lyase.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR020557; Fumarate_lyase_CS.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR022761; Fumarate_lyase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   PANTHER; PTHR11444; PTHR11444; 1.
DR   PANTHER; PTHR11444:SF3; PTHR11444:SF3; 1.
DR   Pfam; PF14698; ASL_C2; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR00838; argH; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006,
KW   ECO:0000256|SAAS:SAAS00067315};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006,
KW   ECO:0000256|SAAS:SAAS00067228};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006562};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006,
KW   ECO:0000256|SAAS:SAAS00067394};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00006,
KW   ECO:0000256|SAAS:SAAS00067331}.
SQ   SEQUENCE   458 AA;  51720 MW;  C67E0B1D20EA7A8A CRC64;
     MKKLWGGRFQ KTPEKWVDEF GASITFDQNL VKEDITGSLA HAAMLKKCGI LTEEEESAIR
     QGLQTLLQKA EEGTLEFSVD YEDIHLNIEK MLIEEIGPLG GKLHTGRSRN DQVATDMHLY
     LKDHVSHIIV LIEQFQKALI EKAEANVETI LPGYTHLQRA QPISFAHHLL AYFWMLERDK
     ERFRDAMKRI NISPLGCGAL AGTTFPIDRN YSAELLGFDS IYENSLDGVS DRDFILEFLS
     SSSMLMMHLS RFSEEIILWC SQEFRFIELD DTYATGSSMM PQKKNPDMAE LIRGKTGRVY
     GDMMGLFTIM KGLPLAYNKD LQEDKEGMFD TVKTVEGSLQ IFTGMIETMT VNKDIMKQAT
     KQDFSNATEL ADYLAKKGMP FREAHEVVGK LVYSCIEKGI YLSDMAFAEF LQASSLFEED
     IYTVLDPHHA VEKRMSAGGT GFQQVKQALV KAKACAGV
//
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