ARLY_PASMU
ID ARLY_PASMU Reviewed; 457 AA.
AC P57909;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 25-MAY-2022, entry version 132.
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}; OrderedLocusNames=PM1120;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03204.1; -; Genomic_DNA.
DR RefSeq; WP_005751835.1; NC_002663.1.
DR AlphaFoldDB; P57909; -.
DR SMR; P57909; -.
DR STRING; 747.DR93_838; -.
DR EnsemblBacteria; AAK03204; AAK03204; PM1120.
DR KEGG; pmu:PM1120; -.
DR PATRIC; fig|272843.6.peg.1133; -.
DR HOGENOM; CLU_027272_2_3_6; -.
DR OMA; KKNPDVF; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000000809; Chromosome.
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;
KW Reference proteome.
FT CHAIN 1..457
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137800"
SQ SEQUENCE 457 AA; 50710 MW; 936CC039B38DBF6A CRC64;
MALWGGRFTQ AADKRFKDFN DSLRFDYRLA EQDIEGSIGW SKALVSVGVL TVQEQQQLES
ALNTLLIEVR SNPQAILQDD AEDIHSWVES KLIDKVGNLG KKLHTGRSRN DQVALDIKMW
CKQRVIELQS SLHALQCKLV ETAENNQHAV MPGYTHLQRA QPITFAHWCM AYVEMLDRDY
SRLTDAYQRM NSCPLGSGAL AGTAYAIDRE QLALDLGFDV ATRNSLDSVS DRDHIVELLS
TASLSMAHLS RFAEDMIIFN SGESNFVELS DRVTSGSSLM PQKKNPDACE LIRGKAGRVM
GALTGMLMTL KGLPLAYNKD MQEDKEGIFD ALDTWQDCID MAALVLDGIQ VNVERTKEAA
LKGYSNATEL ADYLVAKGVP FRDSHHIVGE TVVYAIQQHK ALEALSVAEF KQFSDVVEED
VYQILSLQSC LDKRCAKGGV SPLRVAEAIA EAKARLS
