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Database: UniProt
Entry: A0A0P9A6N6_9PROT
LinkDB: A0A0P9A6N6_9PROT
Original site: A0A0P9A6N6_9PROT 
ID   A0A0P9A6N6_9PROT        Unreviewed;       462 AA.
AC   A0A0P9A6N6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
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=JI56_03260 {ECO:0000313|EMBL:KPU82074.1};
OS   SAR11 cluster bacterium PRT-SC02.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC   Candidatus Pelagibacteraceae.
OX   NCBI_TaxID=1527298 {ECO:0000313|EMBL:KPU82074.1, ECO:0000313|Proteomes:UP000050662};
RN   [1] {ECO:0000313|EMBL:KPU82074.1, ECO:0000313|Proteomes:UP000050662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRT-SC02 {ECO:0000313|EMBL:KPU82074.1};
RA   Leon Zayas R.I., Novotny M., Podell S., Shepard C.M., Berkenpas E.,
RA   Nikolenko S., Pevzner P., Lasken R.S., Bartlett D.H.;
RT   "Microbial Metabolic Properties Below 8,000 Meters Depth Within the Puerto
RT   Rico Trench Inferred From Single Cell Genomes.";
RL   Submitted (AUG-2014) 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}.
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:KPU82074.1}.
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DR   EMBL; JPUP01000093; KPU82074.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P9A6N6; -.
DR   PATRIC; fig|1527298.3.peg.636; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000050662; 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|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00006};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050662}.
FT   DOMAIN          12..299
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          368..437
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   462 AA;  53176 MW;  E4A45B9488A7418E CRC64;
     MTNKNKTVWS NRFKSSTSKS FQRIGSSIKI DKRLYEQDIF ASKVHTQMLI KNKIIPAKEG
     MKIIKGLDKI KNQIQKGKFI FREKFEDIHL NIEKKLHDII GNSAGYMHTA RSRNDQVVTD
     FKLWVKESTL ILINELNSLM KNIIIKAEKN TETVMPGFTH LKNAQPISFA HYLLAYYEMF
     KRDNQRFLNN LNLIDESPLG AAALSGTSYK IDRNFTSKKL GFKKPTNNSI DTVSDRDFAI
     DFLYVCAVCA MHLSRLAEDF IILNSDAYQL ISFSDQMLTG SSIMPQKKNP DPAELIRGRT
     GINYGKLNSI LTIMKGLPIS YFKDLQDDKA LVFDGFDTLK DTLIMSNELI KNIKPNKKRM
     FEMAKSGYTT ATDFADYLVK EKNLSFREAY KISSKIVNYA EKNRKNLDEL TLNEIKRFYK
     DLNISVLKIF DVKNSMNSKN SFGGTSEKNV KNMIKKYKKE LK
//
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