ARLY_BORA1
ID ARLY_BORA1 Reviewed; 470 AA.
AC Q2L1J6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=BAV1635;
OS Bordetella avium (strain 197N).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N;
RX PubMed=16885469; DOI=10.1128/jb.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ49244.1; -; Genomic_DNA.
DR RefSeq; WP_012417306.1; NC_010645.1.
DR AlphaFoldDB; Q2L1J6; -.
DR SMR; Q2L1J6; -.
DR STRING; 360910.BAV1635; -.
DR EnsemblBacteria; CAJ49244; CAJ49244; BAV1635.
DR GeneID; 41393490; -.
DR KEGG; bav:BAV1635; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_4; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 751464at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001977; 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..470
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000240715"
SQ SEQUENCE 470 AA; 51763 MW; 5DC0E12724EB3626 CRC64;
MANTPSQQDQ FANKAQAWSA RFSEPVSDLV KRYTASVDFD KRLARHDIRG SLAHADMLAA
QGIISAQDLA DIERGMQQIL SEIDAGSFQW LLDLEDVHLN IEKRLVELVG DAGKRLHTGR
SRNDQVATDI RLWLRDEIDL LIDLLRQLRH ALATVALDNA GTIMPGFTHL QVAQPVTFGH
HLLAYAEMFG RDAERLADCR KRVNRLPLGA AALAGTSYPI DRERVASTLG FDGVCRNSLD
AVSDRDFAIE FCAAASLIMT HVSRLSEELV LWMSPRVGFI DLADRFCTGS SIMPQKKNPD
VPELARGKTG RVNGHLVALL TLMKGQPLAY NKDNQEDKEG LFDTADTLRD TLTIFADMAG
GIKVKADNMR AAALQGFATA TDLADYLVKR GLPFRDAHEV VAHAVRDCEQ RGCDLADLSL
AELQAYHPSI EADIHQVLTL EGSVAARKHT GGTAPERVRE EAQRVIQETA