ID A0A0C9NJG3_9BACT Unreviewed; 461 AA.
AC A0A0C9NJG3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=BROSI_A0514 {ECO:0000313|EMBL:GAN32010.1};
OS Candidatus Brocadia sinica JPN1.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Brocadiaceae; Brocadia.
OX NCBI_TaxID=1197129 {ECO:0000313|EMBL:GAN32010.1, ECO:0000313|Proteomes:UP000032309};
RN [1] {ECO:0000313|EMBL:GAN32010.1, ECO:0000313|Proteomes:UP000032309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPN1 {ECO:0000313|EMBL:GAN32010.1,
RC ECO:0000313|Proteomes:UP000032309};
RA Oshiki M., Shinyako-Hata K., Satoh H., Okabe S.;
RT "Draft Genome Sequence of an Anaerobic Ammonium-Oxidizing Bacterium,
RT "Candidatus Brocadia sinica".";
RL Genome Announc. 3:e00267-15(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:GAN32010.1}.
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DR EMBL; BAFN01000001; GAN32010.1; -; Genomic_DNA.
DR RefSeq; WP_052562082.1; NZ_BAFN01000001.1.
DR AlphaFoldDB; A0A0C9NJG3; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000032309; 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:GAN32010.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032309}.
FT DOMAIN 9..303
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 366..434
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 461 AA; 52080 MW; 262FBDA649D499EB CRC64;
MKQKKPWGGR FTKQTASSVE SFTESVSFDW RLYQYDIEGS IAHATMLAKC KLITEKEKDA
IVKGLKEILA EIEAEKFEFK KSLEDVHMNI ESALIERIGE AGKKLHTARS RNDQVALDLR
LWTRNQTRET IGLLAALQKE FVRKGKAVFG LIMPGFTHLQ HAQPVLVSHY LLAYVEMLER
DKTRLQDCLA RLNKSPLGAC ALAGTTLPTD PAFTAKLLDF DGVYENSMDA VSDRDFCVEY
AFCLSLVAVH LSRLCEEWII WCNDEVKFIE ISDAYCTGSS IMPQKKNPDV LELIRGKCGR
AFGHLTSLLT LLKGLPLSYN RDMQEDKMAI FDASDTVQTS LSVLTELVAN TNFHGERMML
ACEKGFIDAT ALAEYLVKKG VPFRMAHEIV GKIVRECIRV QCRLMDLRLE SFKAFSSVIE
KDVYKVLGVE NCIKNYKSHG STAPGFVKKR IAYWEKKLSK G
//
