ID H6N115_GORPV Unreviewed; 490 AA.
AC H6N115;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Aspartate ammonia-lyase AspA {ECO:0000313|EMBL:AFA74578.1};
DE EC=4.3.1.1 {ECO:0000313|EMBL:AFA74578.1};
GN Name=aspA {ECO:0000313|EMBL:AFA74578.1};
GN OrderedLocusNames=GPOL_c35660 {ECO:0000313|EMBL:AFA74578.1};
OS Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA74578.1, ECO:0000313|Proteomes:UP000009154};
RN [1] {ECO:0000313|EMBL:AFA74578.1, ECO:0000313|Proteomes:UP000009154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RX PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A.,
RA Liebl W., Daniel R., Steinbuchel A.;
RT "Involvement of two latex-clearing proteins during rubber degradation and
RT insights into the subsequent degradation pathway revealed by the genome
RT sequence of Gordonia polyisoprenivorans strain VH2.";
RL Appl. Environ. Microbiol. 78:2874-2887(2012).
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DR EMBL; CP003119; AFA74578.1; -; Genomic_DNA.
DR AlphaFoldDB; H6N115; -.
DR STRING; 1112204.GPOL_c35660; -.
DR KEGG; gpo:GPOL_c35660; -.
DR eggNOG; COG1027; Bacteria.
DR HOGENOM; CLU_021594_4_0_11; -.
DR Proteomes; UP000009154; Chromosome.
DR GO; GO:0008797; F:aspartate ammonia-lyase activity; IEA:UniProtKB-EC.
DR CDD; cd01357; Aspartase; 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; 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; PTHR42696; ASPARTATE AMMONIA-LYASE; 1.
DR PANTHER; PTHR42696:SF2; ASPARTATE AMMONIA-LYASE; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:AFA74578.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009154}.
FT DOMAIN 14..345
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT REGION 438..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 490 AA; 52263 MW; 42D369FB620EC562 CRC64;
MTMAQKRAET DLLGRREVPA EAYWGIHTLR AVENFPVTGR TIGSNAHLVR ALAAVKWSAA
RANADLGILD EERASAICAA CDEILDGGFH DQFVVDVIQG GAGTSTNMNA NEVIANRALE
ILGHGRGEYR HLHPNEHVNA GQSTNDVYPT AVNVATIRAV GELDEAMSVL QQAFARKAAE
FSSVVKMGRT QLQDAVPMTL GQEFGAFAVM IDEDRQRLRE AAILVHEINL GATAIGTGLN
APIGYADKAV GYLRDKTGLD LVSAHDLVEA TQDVGQFVHL SGVLKRVAVK LSKICNDLRL
LSSGPRAGLG EINLPPVQAG SSIMPGKVNP VIPEVVSQVA YEVIGNDVTI TMAAESGQLQ
LNAFEPIILT CLSDGMTHLS AACRTLAARC VDGITANEET LRHRVENSIG LVTALSPSLG
YVASTRNRPG GVAQWAYRPR IGSRGGPPRA RRTRTTAQPF ASGQSASGDR RGRQHPLRTG
DENPDVSGVW
//
