ID A0A0S8B160_9BACT Unreviewed; 459 AA.
AC A0A0S8B160;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=AMS20_06920 {ECO:0000313|EMBL:KPK05305.1};
OS Gemmatimonas sp. SG8_28.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=1703357 {ECO:0000313|EMBL:KPK05305.1, ECO:0000313|Proteomes:UP000051120};
RN [1] {ECO:0000313|EMBL:KPK05305.1, ECO:0000313|Proteomes:UP000051120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_28 {ECO:0000313|EMBL:KPK05305.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPK05305.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJNQ01000096; KPK05305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8B160; -.
DR PATRIC; fig|1703357.3.peg.264; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000051120; 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; 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.
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}.
FT DOMAIN 4..296
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 360..427
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 459 AA; 49508 MW; 1E8D063E20F88E35 CRC64;
MWGGRFTGAL SDAAAELNRS LPVDRRLWRQ DVRVAQAWVS ALAVAGIIAP AEERTLADGL
RRVAERLADG ADAHAPDEDV HTLVERLLYE EVGEIAGKLN TGRSRNDQVA TDLRLWCLEA
AASVRQEVTA LATVLAERAS AGIDVLLPGY THGQRAQPVR WAYVLLAHAW PLIRDLQRLN
EVSDRTGELP LGAGAVAGSF VPIDRERLCE ILGFRRIAAN SLDVTGDRDF VADLVHALAM
VSVHLSRLCG EFAVYTSSEY GFVRLDDAYS TGSSLLPQKR NPDIFELARA KSARVVAALS
GLLNLLRGLP AGYSKDLQED KAFLFDAVDT LLLTLPAVRG AIETLQPVPD RMRAALSSSL
LATDLADGLA GEGVPFREAH AVVGRLVRHA EAQGIELRTI TEADAAALHP SLPRLIAAVG
TFEDSVERRR TTGGASREAV ARQLREVRSS LAKPGGTRP
//