ID V9XCB4_9NOCA Unreviewed; 473 AA.
AC V9XCB4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=argH {ECO:0000256|HAMAP-Rule:MF_00006};
GN ORFNames=Y013_04710 {ECO:0000313|EMBL:AHD20023.1};
OS Rhodococcus pyridinivorans SB3094.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD20023.1, ECO:0000313|Proteomes:UP000018781};
RN [1] {ECO:0000313|EMBL:AHD20023.1, ECO:0000313|Proteomes:UP000018781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3094 {ECO:0000313|EMBL:AHD20023.1,
RC ECO:0000313|Proteomes:UP000018781};
RX PubMed=24874690;
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA Nielsen P.H., Nielsen J.L.;
RT "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL Genome Announc. 2:e00525-14(2014).
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; CP006996; AHD20023.1; -; Genomic_DNA.
DR RefSeq; WP_006554816.1; NC_023150.1.
DR AlphaFoldDB; V9XCB4; -.
DR GeneID; 29937498; -.
DR KEGG; rpy:Y013_04710; -.
DR PATRIC; fig|1435356.3.peg.941; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_2_11; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000018781; 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; 1.10.40.30; 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|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW 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:AHD20023.1}.
FT DOMAIN 21..309
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 372..440
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 473 AA; 50097 MW; 10942AC5F1F0FCB3 CRC64;
MTAHGTNEGA LWGGRFASGP AAAMAALSKS THFDWALAPY DVRASQAHAK VLHRAGLLTD
DDLATMLDGL DRLAADVASG AFGPAESDED VHGALERGLI ERVGPEVGGR LRAGRSRNDQ
VATLFRMWLR DSARRIADGV LDVVDAIADQ AAAHPDAVMP GKTHLQAAQP VLLAHHLLAH
AHPLLRDVDR LRDFDKRAAV SPYGSGALAG SSLGLDPDAI AADLGFDSAA DNSIDATSSR
DFAAEAAFVF AQIAVDLSRM AEEIILWSTP EFGYVTLADE WSTGSSIMPQ KKNPDVSELT
RGKAGRLIGN LTGLLATLKA QPLAYNRDLQ EDKEPVFDSV AQLELLLPAI AGLVSTLTFH
TERMAELAPA GFTLATDIAE WMVRQGVPFR VAHEAAGACV RVAEGRGAGL EDLTDEELAG
VDPALTPQVR EVLTVEGSIA SRDARGGTAG VRVAEQLGRV RDAAAQLRDR VRD
//
