ID A0A3P4B5K0_9BURK Unreviewed; 474 AA.
AC A0A3P4B5K0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Argininosuccinate lyase {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE Short=ASAL {ECO:0000256|HAMAP-Rule:MF_00006};
DE EC=4.3.2.1 {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE AltName: Full=Arginosuccinase {ECO:0000256|HAMAP-Rule:MF_00006};
GN Name=argH1 {ECO:0000313|EMBL:VCU71584.1};
GN Synonyms=argH {ECO:0000256|HAMAP-Rule:MF_00006};
GN ORFNames=PIGHUM_03669 {ECO:0000313|EMBL:VCU71584.1};
OS Pigmentiphaga humi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pigmentiphaga.
OX NCBI_TaxID=2478468 {ECO:0000313|EMBL:VCU71584.1, ECO:0000313|Proteomes:UP000277294};
RN [1] {ECO:0000313|EMBL:VCU71584.1, ECO:0000313|Proteomes:UP000277294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DnA1 {ECO:0000313|EMBL:VCU71584.1};
RA Criscuolo A.;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00000985, ECO:0000256|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.
CC {ECO:0000256|ARBA:ARBA00004941, ECO:0000256|HAMAP-Rule:MF_00006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00006}.
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DR EMBL; UWPJ01000027; VCU71584.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P4B5K0; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000277294; Unassembled WGS sequence.
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; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 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 NCBIfam; TIGR00838; argH; 1.
DR PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_00006}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000313|EMBL:VCU71584.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000277294}.
FT DOMAIN 23..316
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 379..447
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
FT REGION 449..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 52302 MW; 17F9BB146D8A27F1 CRC64;
MSTPTDPRPQ DQFAKKAEAW SARFSEPVSD LVKRYTASVD FDKRLAKFDI QGSLAHAEML
QSVGILTHQD LDDIRRGMAA IESEIDAGRF EWLLDLEDVH LNIERRLTEL VGDAGKRLHT
GRSRNDQVAT DIRLWLRAEI DTLLDLLGQL RRALATLALE HAGTIMPGFT HLQVAQPVTF
GHHLLAYAEM FGRDAERLAD CRKRVNRLPL GAAALAGTSY PIDRERVART LGFDGVCRNS
LDAVSDRDFA IEFCAAGALV MTHISRLSEE LVLWMSPRVG FIDLADRFCT GSSIMPQKKN
PDVPELARGK TGRVNGHLVA LLTLMKGQPL AYNKDNQEDK EGLFDTADTV RDTLRIFIDM
AAGIQVKPEA MRAAALQGFS TATDLADYLV KKGVPFRDAH EAVALAVRQC VERNCDLADL
SVDELRAFHP SVGDDVHGVL TLEGSVASRS HVGGTAPERV REEAQRVLSP PPTR
//
