ID C0QA12_DESAH Unreviewed; 386 AA.
AC C0QA12;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=ArnB {ECO:0000313|EMBL:ACN16730.1};
DE EC=2.6.1.- {ECO:0000313|EMBL:ACN16730.1};
GN Name=arnB {ECO:0000313|EMBL:ACN16730.1};
GN OrderedLocusNames=HRM2_36720 {ECO:0000313|EMBL:ACN16730.1};
OS Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS HRM2) (Desulfobacterium autotrophicum).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulforapulum.
OX NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN16730.1, ECO:0000313|Proteomes:UP000000442};
RN [1] {ECO:0000313|EMBL:ACN16730.1, ECO:0000313|Proteomes:UP000000442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC {ECO:0000313|Proteomes:UP000000442};
RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA Meyerdierks A., Gottschalk G., Amann R.;
RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT reducer oxidizing organic carbon completely to carbon dioxide.";
RL Environ. Microbiol. 11:1038-1055(2009).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP001087; ACN16730.1; -; Genomic_DNA.
DR RefSeq; WP_015905479.1; NC_012108.1.
DR AlphaFoldDB; C0QA12; -.
DR STRING; 177437.HRM2_36720; -.
DR KEGG; dat:HRM2_36720; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_7_2_7; -.
DR OrthoDB; 9771070at2; -.
DR Proteomes; UP000000442; Chromosome.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR020026; PseC.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR03588; PseC; 1.
DR PANTHER; PTHR30244:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ACN16730.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000000442};
KW Transferase {ECO:0000313|EMBL:ACN16730.1}.
FT ACT_SITE 189
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 189
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 386 AA; 43590 MW; FB4D28ADD12510D7 CRC64;
MISQKSAENY IPYGRQSIDE EDIQAVVNIL KSDWLTTGPQ IEKFEKAFCS FTNANEAVAV
SSGTAALHAA MNAINIQPGD EVIVPPMTFA ATANAVVYQG GTPVFADVLP DTLLINPEEV
KKKITSRTKA IIAVDYAGQS CDYDALRFIS DKHKLYLITD ACHALGGRYK GRKIGSLADL
TLFSFHPVKH ITTGEGGMIT CSDSTLAAKM KTFRNHGITT DQHRRSMEGT WYYEMESLGY
NYRITDIQCA LGLSQLKKLD GWIKNRNWIA RKYDKAFSEE ESISPLKVMK EMVHAYHLYV
IKLPDRKLRD TVYKEMHRHN IGVNVHYIPV HLHPYYRKTF NTSQGLCPVA EDAFQRILSL
PMHPKINNTD IKRIVTELTN AIEKNR
//
