ARLY_VIBC3
ID ARLY_VIBC3 Reviewed; 458 AA.
AC A5F4Z3; C3LXN9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Argininosuccinate lyase {ECO:0000255|HAMAP-Rule:MF_00006};
DE Short=ASAL {ECO:0000255|HAMAP-Rule:MF_00006};
DE EC=4.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00006};
DE AltName: Full=Arginosuccinase {ECO:0000255|HAMAP-Rule:MF_00006};
GN Name=argH {ECO:0000255|HAMAP-Rule:MF_00006};
GN OrderedLocusNames=VC0395_A2217, VC395_2754;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(N(omega)-L-arginino)succinate = fumarate + L-arginine;
CC Xref=Rhea:RHEA:24020, ChEBI:CHEBI:29806, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:57472; EC=4.3.2.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00006};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 3/3. {ECO:0000255|HAMAP-
CC Rule:MF_00006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00006}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00006}.
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DR EMBL; CP000627; ABQ19766.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP10739.1; -; Genomic_DNA.
DR RefSeq; WP_001240133.1; NZ_JAACZH010000007.1.
DR AlphaFoldDB; A5F4Z3; -.
DR SMR; A5F4Z3; -.
DR STRING; 345073.VC395_2754; -.
DR EnsemblBacteria; ABQ19766; ABQ19766; VC0395_A2217.
DR KEGG; vco:VC0395_A2217; -.
DR KEGG; vcr:VC395_2754; -.
DR PATRIC; fig|345073.21.peg.2653; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_6; -.
DR OMA; KKNPDVF; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000000249; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR CDD; cd01359; Argininosuccinate_lyase; 1.
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; PTHR43814; PTHR43814; 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; Arginine biosynthesis; Cytoplasm; Lyase.
FT CHAIN 1..458
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000070923"
SQ SEQUENCE 458 AA; 50331 MW; F1BA176B23D61B9C CRC64;
MALWGGRFTQ AADSRFKSFN DSLRFDYRLA EQDIVGSIAW SKALVSVNVL SVQEQQQLEQ
ALNHLLQSVQ QDPEQILASD AEDIHSWVEQ KLIEQVGDLG KKLHTGRSRN DQVATDLKLW
CRDQGVHLLL ALKTLQQQLV AVAAEHQSTV LPGYTHLQRA QPVTFTHWCL AYLEMFERDE
SRLTDALARL NTSPLGSGAL AGTAYAIDRE VLAADLGFTR ATRNSLDAVS DRDHVMELMS
VASISMLHLS RLAEDMIFYT TGEAGFIELA DTVTSGSSLM PQKKNPDALE LIRGKTGRVY
GALAGMMMTV KALPLAYNKD MQEDKEGLFD ALDTWFDCLQ MAGLCFDGIK VNAARTLEAA
KQGYSNATEL ADYLVAKGIP FREAHHIVGV AVVAAIGKGV ALEELCLAEL QQFSPLIEQD
VYPILTIESC LEKRCALGGV SPKQVAHALQ QAQARVKS