ID I0I960_CALAS Unreviewed; 446 AA.
AC I0I960;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000313|EMBL:BAM01798.1};
GN Name=hemL {ECO:0000313|EMBL:BAM01798.1};
GN OrderedLocusNames=CLDAP_37580 {ECO:0000313|EMBL:BAM01798.1};
OS Caldilinea aerophila (strain DSM 14535 / JCM 11387 / NBRC 104270 /
OS STL-6-O1).
OC Bacteria; Chloroflexota; Caldilineae; Caldilineales; Caldilineaceae;
OC Caldilinea.
OX NCBI_TaxID=926550 {ECO:0000313|EMBL:BAM01798.1, ECO:0000313|Proteomes:UP000007880};
RN [1] {ECO:0000313|EMBL:BAM01798.1, ECO:0000313|Proteomes:UP000007880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1
RC {ECO:0000313|Proteomes:UP000007880};
RA Oguchi A., Hosoyama A., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA Hanada S., Yamazaki S., Fujita N.;
RT "Complete genome sequence of Caldilinea aerophila DSM 14535 (= NBRC
RT 102666).";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; AP012337; BAM01798.1; -; Genomic_DNA.
DR RefSeq; WP_014435021.1; NC_017079.1.
DR AlphaFoldDB; I0I960; -.
DR STRING; 926550.CLDAP_37580; -.
DR KEGG; cap:CLDAP_37580; -.
DR PATRIC; fig|926550.5.peg.4044; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_0; -.
DR OrthoDB; 9807885at2; -.
DR Proteomes; UP000007880; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; NF041362; GntE_guanitoxin; 1.
DR PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000007880}.
SQ SEQUENCE 446 AA; 49412 MW; 41AF5D4590ECB6D5 CRC64;
MNPVKTRTHQ LFAKAKQYIP YGVNSNFRYW GDENTPILTR GAGAYVWDAD DNRYIDYRLG
FGPIILGHAY PEVTRRVAEA IQNGVLFAAT TPIEIELAER FTRMTGMDKV RLSNTGTEAN
MHALRIARAY TGREKFIKFE GNYHGNFDYV MFSGPTAKAE LLGPRNHPHR LRATEGMPVA
IRNYMISLPY NDIELLERAM VEHSDELAAV IVEPIMGNVA CILPDPAWLR RVRELCDEFD
IVLIFDEVKT GFRLAPGGAQ QYFGVKADLA AYAKAMGNGF PVSAVAGREE IMAVVEPGRV
AHGGTYCGNV VAATAAAATL EIIETQPVIE TIFANGRRLI DGIHTILRQV GAPHVISGVP
SMFSVLLGKD EPPTDYRSYA EFDSELFGLF GAELIRRGVL IDDDPREPWF LSFSHDAAVI
DESLNLIEDA AKAVFRTAAR TRRLAA
//
