ID Q9HRM6_HALSA Unreviewed; 380 AA.
AC Q9HRM6;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN Name=aspB2 {ECO:0000313|EMBL:AAG19132.1};
GN Synonyms=aspC2 {ECO:0000313|EMBL:DAC77837.1};
GN OrderedLocusNames=VNG_0629G {ECO:0000313|EMBL:AAG19132.1};
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium; Halobacterium salinarum NRC-34001.
OX NCBI_TaxID=64091 {ECO:0000313|EMBL:AAG19132.1, ECO:0000313|Proteomes:UP000000554};
RN [1] {ECO:0000313|EMBL:AAG19132.1, ECO:0000313|Proteomes:UP000000554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1
RC {ECO:0000313|Proteomes:UP000000554}, and NRC-1
RC {ECO:0000313|EMBL:AAG19132.1};
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.W., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [2] {ECO:0000313|EMBL:DAC77837.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRC-1 {ECO:0000313|EMBL:DAC77837.1};
RX PubMed=18313895; DOI=.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
RN [3] {ECO:0000313|EMBL:DAC77837.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRC-1 {ECO:0000313|EMBL:DAC77837.1};
RX PubMed=26042526;
RA Pfeiffer F., Oesterhelt D.;
RT "A manual curation strategy to improve genome annotation: application to a
RT set of haloarchael genomes.";
RL Life 5:1427-1444(2015).
RN [4] {ECO:0000313|EMBL:DAC77837.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRC-1 {ECO:0000313|EMBL:DAC77837.1};
RA Pfeiffer F., Marchfelder A., Habermann B.H., Dyall-Smith M.;
RT "The genome of the Halobacterium salinarum type strain is closely related
RT to that of the laboratory strains NRC-1 and R1.";
RL Microbiol. Resour. Announc. 0:0-0(2019).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000481};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
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DR EMBL; AE004437; AAG19132.1; -; Genomic_DNA.
DR EMBL; BK010829; DAC77837.1; -; Genomic_DNA.
DR PIR; H84220; H84220.
DR RefSeq; WP_010902428.1; NC_002607.1.
DR AlphaFoldDB; Q9HRM6; -.
DR STRING; 64091.VNG_0629G; -.
DR PaxDb; 64091-VNG_0629G; -.
DR GeneID; 68693513; -.
DR KEGG; hal:VNG_0629G; -.
DR PATRIC; fig|64091.14.peg.479; -.
DR HOGENOM; CLU_017584_4_3_2; -.
DR OrthoDB; 372018at2157; -.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:AAG19132.1};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Reference proteome {ECO:0000313|Proteomes:UP000000554};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:DAC77837.1}.
FT DOMAIN 31..374
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 380 AA; 40192 MW; DA09A1E219CCBA9D CRC64;
MNFSTRVTSV EPSATLAVST LASELEADGV DVVDLSVGEP DFDTPESIVD AGKAAMDAGH
TGYAPSNGVP ELRDAIAEKL QGDGLDYEAG NVIVTPGAKQ ALYETFQAVV DEGDEVALLD
PAWVSYEAMA KLAGGELNRV DLAPHDFQLE PALDDLADAV SDDTELLVVN SPSNPTGAVY
SRAAMEGVRD LAVDHDITVI SDEIYQRVNY GPAHVSLAGL DGMFERTVTI NGFSKAYSMT
GWRLGYLAGP EALVDQAGKV QSHSVSSAAN FIQRAGVEAI RHTDDAIDEM VAAFESRRDL
LVDLFAEHGT DVSTPDGAFY LMLPVADDDQ AWCQDALKDA HVATVPGSAF GAPGYARLSY
AASTDRLEAA VDRLAAEGYL
//
