ID A0A4R3L0F1_9BACL Unreviewed; 413 AA.
AC A0A4R3L0F1;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 02-APR-2025, entry version 13.
DE SubName: Full=Argininosuccinate lyase {ECO:0000313|EMBL:TCS92399.1};
GN ORFNames=EDD58_11222 {ECO:0000313|EMBL:TCS92399.1};
OS Hazenella coriacea.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
OC Thermoactinomycetaceae; Hazenella.
OX NCBI_TaxID=1179467 {ECO:0000313|EMBL:TCS92399.1, ECO:0000313|Proteomes:UP000294937};
RN [1] {ECO:0000313|EMBL:TCS92399.1, ECO:0000313|Proteomes:UP000294937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45707 {ECO:0000313|EMBL:TCS92399.1,
RC ECO:0000313|Proteomes:UP000294937};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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:TCS92399.1}.
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DR EMBL; SMAG01000012; TCS92399.1; -; Genomic_DNA.
DR RefSeq; WP_131926698.1; NZ_SMAG01000012.1.
DR AlphaFoldDB; A0A4R3L0F1; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000294937; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR052032; ATP-dep_AA_Ligase.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR040570; LAL_C2.
DR PANTHER; PTHR43585:SF2; ATP-GRASP ENZYME FSQD; 1.
DR PANTHER; PTHR43585; FUMIPYRROLE BIOSYNTHESIS PROTEIN C; 1.
DR Pfam; PF13535; ATP-grasp_4; 1.
DR Pfam; PF18603; LAL_C2; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lyase {ECO:0000313|EMBL:TCS92399.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000294937}.
FT DOMAIN 115..314
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 413 AA; 45913 MW; 084714AE3E623136 CRC64;
MEQYLLFIES NTTGTGMIAI VRAKELGFSP IFITNNPQRY KGLTETECKV IQCDTHSLSE
IQQAITEKIE TNHIAGITTT SDFYLETVAQ LQKIYQLPGN SPEAIRACRH KGLMRQALER
SPLIQPRFMM VRSVEEWENA ARYMTFPCIV KPVDDSGSNE VKLCHHMKEV SEQVSRIVAI
QANVRGQATA QTALIEEYLE GPEYSVEMFS DQQGTHCIGI TQKEVMGKPY FVECGHLFPA
LLSKVQEQQI IEAVQTALEI VGYQFGPSHT EVRWTAQGPA IIEINARLAG GMIPELIRLA
TGMDLLEQQI LTATGKNVEL SHENKRVAGI TFIMADQLGV LTDYQGTELA EQVAGIQLVK
LTATKGSQVL PPQNAYHRLG YLIAAGDSHQ QVQQSLAQAT TKIQLHIEHH KEG
//