ID A1UR01_BARBK Unreviewed; 1569 AA.
AC A1UR01;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Glutamate dehydrogenase, NAD-specific {ECO:0000313|EMBL:ABM45117.1};
GN OrderedLocusNames=BARBAKC583_0066 {ECO:0000313|EMBL:ABM45117.1};
OS Bartonella bacilliformis (strain ATCC 35685 / KC583 / Herrer 020/F12,63).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=360095 {ECO:0000313|EMBL:ABM45117.1, ECO:0000313|Proteomes:UP000000643};
RN [1] {ECO:0000313|EMBL:ABM45117.1, ECO:0000313|Proteomes:UP000000643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35685 / NCTC 12138 / KC583
RC {ECO:0000313|Proteomes:UP000000643};
RA Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA Fraser-Ligget C., Seshadri R.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000524; ABM45117.1; -; Genomic_DNA.
DR RefSeq; WP_005765796.1; NC_008783.1.
DR STRING; 360095.BARBAKC583_0066; -.
DR GeneID; 72471640; -.
DR KEGG; bbk:BARBAKC583_0066; -.
DR PATRIC; fig|360095.6.peg.65; -.
DR eggNOG; COG2902; Bacteria.
DR HOGENOM; CLU_003404_1_1_5; -.
DR OrthoDB; 9758052at2; -.
DR Proteomes; UP000000643; Chromosome.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR048381; GDH_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR028971; NAD-GDH_cat.
DR InterPro; IPR049062; NAD_Glu_DH_ACT2.
DR InterPro; IPR049064; NAD_Glu_DH_ACT3.
DR InterPro; IPR007780; NAD_Glu_DH_bac.
DR InterPro; IPR049059; NAD_Glu_DH_HM1.
DR InterPro; IPR049056; NAD_Glu_DH_HM3.
DR InterPro; IPR024727; NAD_Glu_DH_N_ACT1.
DR PANTHER; PTHR43403; NAD-SPECIFIC GLUTAMATE DEHYDROGENASE; 1.
DR PANTHER; PTHR43403:SF1; NAD-SPECIFIC GLUTAMATE DEHYDROGENASE; 1.
DR Pfam; PF05088; Bac_GDH_CD; 1.
DR Pfam; PF21075; GDH_ACT1; 1.
DR Pfam; PF21076; GDH_ACT2; 1.
DR Pfam; PF21077; GDH_ACT3; 1.
DR Pfam; PF21074; GDH_C; 1.
DR Pfam; PF21073; GDH_HM1; 1.
DR Pfam; PF21078; GDH_HM3; 1.
DR PIRSF; PIRSF036761; GDH_Mll4104; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000643}.
FT DOMAIN 20..132
FT /note="NAD-glutamate dehydrogenase N-terminal ACT1"
FT /evidence="ECO:0000259|Pfam:PF21075"
FT DOMAIN 368..458
FT /note="NAD-glutamate dehydrogenase ACT2"
FT /evidence="ECO:0000259|Pfam:PF21076"
FT DOMAIN 512..579
FT /note="NAD-glutamate dehydrogenase ACT3"
FT /evidence="ECO:0000259|Pfam:PF21077"
FT DOMAIN 687..1182
FT /note="NAD-glutamate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05088"
FT DOMAIN 1227..1555
FT /note="NAD-specific glutamate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21074"
SQ SEQUENCE 1569 AA; 177313 MW; 380BDCC4A61F3809 CRC64;
MSKQEILDIK KDPNEIESIL FAHADEEDRA RYKSSELQKA AKVATEALHQ YRRGESTVCF
EHTLTCNDKP ITIVTLVNDN KPFLLDSILN VFNQQINKIY LIAHPVLDCA SEQRISLIQI
HVEALNQQQT QKLKDEITLV LGQVNAAVQD WQPMLEQVKK CIHAYQTNLP LNYQKEGAKT
IEFLQWLMNN NFIFLGLRTY DFTEGQNPDK ALNAGDIELG ILTDASIRII ENAHMGESPQ
ELLSFMESDA LFTVTKANSR SKIHRFVRLD YIGLKIFNKA GLLCGEMRIV GLFTSSAYTH
SILTIPFLKE KAETIIQRLG YNRADHSGKA LISVLETYPR DEMFHSDVDT LTENAKLILQ
LDERPRLRVL AHADSFGRFV SVLVYVPRDQ YGSSKREKIG AYLVDIYEGD FFESYPLFLE
STLIRIHYIV YRKSNQSAPV IERTTLEHAV REITRNWEET VQAVALAHKA TDQQTHLASQ
FPNSYRDLFS AEDAINDAAH ILNLNDQHPL FVTFYHTHHK EKHTIALRLF HRHEALALSK
RVPLLENMGF RVIAEQTLEL PDSNGKYVYL HDMQLESSFQ ICVNLDENGL KLAETFEAVW
AQNADDDAFN ALTQTAQLDW REIVILRHYG RYIQQAGIPY SQERVAKTLN AYPHITQDLY
ALFHLKFHQS HTAEERQKNE TIIQQRIEEK LQHVPSLDDD LILRRYRNLI AASLRTNAFT
PLADGSPRRI LATKLDPRQI EGLPEPRPYR EIFVYGPEVE GVHLRFGPIA RGGIRWSDRA
LDYRTEVLDL VKAQQVKNAV IVPVGAKGGF YPHCLPQTDN RSVVVEAARQ AYISYIAALL
SITDNLVDGK VKAAPNVIRH DGDDPYFVVA ADKGTATFSD TANAISQENH FWLDDAFASG
GSAGYDHKAI GITAKGAWEA VKRHFRESFD HDIQTKPFTC VGVGDMSGDV FGNGLLLSQQ
TKLIAAFDHR DIFIDPDPNA AESYAERMRL FQLPRSSWQD YDQGKLSKGG GVFSRTAKTI
TLSREAAQAI GFEKQTGTPF EIITAILKAP VDLLWFGGIG TYVRATTETN AQVGDRTNDA
VRITGEQVRA KVIGEGANLG LTQRGRIEYI LNGGRCNTDA IDNSAGVNCS DVEVNIKIVL
ASALQAKKLT RDARDALLKE MTPQVEQLVL RNNYLQPLAL SLAEKRGVLD LPYQARFIND
LEKKNLLDRR VEILPDEQIL RQRLAQNQGL TRPELAVILA YAKLTLQEEI ANNPIVDHHY
FDSTLLGYFP TQLQTQFEQE IINHQLRRHI IATLIANDIV NRGGPTFVNR LQDKTGQKVE
NIIRVFIAIR DGFEIPQLSN QIDNLDNKIP GLIQNKLYAS ITSMLFEATN WGLRHMDLST
PLEDLVKTIK QARTVIEEQL THSNGRDIHQ KIAKKAASYC KEGAPKALAQ HLALLEVASI
ICDISLIAKQ NKSDLIQTAQ IYFSLAQIIH INRIDEASRA IPIFDYYDGM ALSQAKENIA
ESLRQIVTKI LQNYGEQNDP LAVWIKTEEN QIYTVTNRIG TLIEGDLNIS RFTFAASMIA
QLKNTTFQS
//
