ID C3MHA8_SINFN Unreviewed; 445 AA.
AC C3MHA8;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Adenylosuccinate lyase {ECO:0000313|EMBL:ACP26394.1};
DE EC=4.3.2.2 {ECO:0000313|EMBL:ACP26394.1};
GN OrderedLocusNames=NGR_c26380 {ECO:0000313|EMBL:ACP26394.1};
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394 {ECO:0000313|EMBL:ACP26394.1, ECO:0000313|Proteomes:UP000001054};
RN [1] {ECO:0000313|EMBL:ACP26394.1, ECO:0000313|Proteomes:UP000001054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
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DR EMBL; CP001389; ACP26394.1; -; Genomic_DNA.
DR RefSeq; WP_012709151.1; NC_012587.1.
DR RefSeq; YP_002827147.1; NC_012587.1.
DR AlphaFoldDB; C3MHA8; -.
DR STRING; 394.NGR_c26380; -.
DR KEGG; rhi:NGR_c26380; -.
DR PATRIC; fig|394.7.peg.5464; -.
DR eggNOG; COG0015; Bacteria.
DR HOGENOM; CLU_030949_0_0_5; -.
DR OrthoDB; 9768878at2; -.
DR Proteomes; UP000001054; Chromosome.
DR GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IEA:UniProtKB-EC.
DR CDD; cd01597; pCLME; 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 InterPro; IPR019468; AdenyloSucc_lyase_C.
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 PANTHER; PTHR43172; ADENYLOSUCCINATE LYASE; 1.
DR Pfam; PF10397; ADSL_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SMART; SM00998; ADSL_C; 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:ACP26394.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT DOMAIN 364..440
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
SQ SEQUENCE 445 AA; 48692 MW; 9A2C567023F80268 CRC64;
MTIGMFSSFI TRHWFSEVAI DIWSDEATLQ AWLDVEAALA LAQAKLVLIP PEPAERIAAC
CDAKGFDYER LSKEIAFAQH PFVPVLKQLE ELCGEPAAGF IHWGATTQNI FDTAIALQLK
KTHLHLIAVL ERTEERLKGL AFEHRQTLQA GRTHGQHALP MTFGFKVAGW HEEIRRSRER
LAARGKTSFL AYFGGAIGTF AAMDGKGRAV EDEAARLLGL QPARLPLRSS FDRVTDYLAA
LAVLAGSIHK IAQDIVFMQR SEIGEIEEAF HMGKVGSSTM AQKRNPSAAL VLVSLCRMLE
GRLPMVLAAM VRMDEGDSSA TNIADIVVGE IAVLAASIAE GADRVLSGLH VNAEKMRRNL
DLSRGLILSE SAMMQLSPRI GRHKAHHLLY EAAQRTAMEG TAFSQTLADA MKDAGLADVE
LDLSPDDYLG EIGEIIEDLC TPRRG
//
