ID G5SWQ3_9BACT Unreviewed; 518 AA.
AC G5SWQ3;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=HMGL-like protein {ECO:0000313|EMBL:EHG98284.1};
GN ORFNames=HMPREF9441_03826 {ECO:0000313|EMBL:EHG98284.1};
OS Paraprevotella clara YIT 11840.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Paraprevotella.
OX NCBI_TaxID=762968 {ECO:0000313|EMBL:EHG98284.1, ECO:0000313|Proteomes:UP000003598};
RN [1] {ECO:0000313|EMBL:EHG98284.1, ECO:0000313|Proteomes:UP000003598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11840 {ECO:0000313|EMBL:EHG98284.1,
RC ECO:0000313|Proteomes:UP000003598};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|RuleBase:RU003523}.
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:EHG98284.1}.
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DR EMBL; AFFY01000098; EHG98284.1; -; Genomic_DNA.
DR RefSeq; WP_008623075.1; NZ_JH376661.1.
DR AlphaFoldDB; G5SWQ3; -.
DR STRING; 762968.HMPREF9441_03826; -.
DR GeneID; 78584502; -.
DR PATRIC; fig|762968.3.peg.3344; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_0_1_10; -.
DR OrthoDB; 9804858at2; -.
DR Proteomes; UP000003598; Unassembled WGS sequence.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.160.340; -; 1.
DR Gene3D; 3.30.160.740; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR10277:SF57; (R)-CITRAMALATE SYNTHASE CIMA; 1.
DR PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 8..269
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 518 AA; 57991 MW; CC311322BEEC3FC4 CRC64;
MKANPVKIEI MDTTLRDGEQ TSGVSFVPHE KLMIARALLQ DLNVDRIEVA SARVSEGEVD
AVRSICQWAR QTGRLHRVEV LGFVDGHASL DWIHACGCKN INLLCKGSEN HCTNQLKKTL
EQHVADIRRS LDYAEELGIA VNVYLEDWSN GMKHSPDYVF ALMDALKDTK IRRFMLPDTL
GILNPLDLLG YIRKMVKRYP GLHFDFHAHN DYDLAISNVL AAVLGGCRGI HTSVNGLGER
AGNAPLASVQ AILKDQFNAQ TDIDESRLNE VSRMVESYSG IPIPPNRPIT GESVFTQVAG
VHADGDNKAN LYCNDLLPER FGRKREYALG KNSGKANILK NLEELGLELS PEQTRKVTER
IIELGDKKEL VTQEDLPYIV SDVLKHDTVE EHVRLLSYMV TTAYGLKPMA QVKLEINGEA
YEENASGDGQ FDAFMRAARH IYKNRLSRKF PWLANYSVSI PPGGRTDALV QAVITWNWNG
KVYRTRGLDA DQTEAAIKAT VKLLNLIEED YKDLESHV
//
