P45353

PR
Gene name
HIS4
Protein name
Histidine biosynthesis trifunctional protein
Names
Species
Komagataella pastoris (Yeast) (Pichia pastoris)
KEGG Pathway
EC number
1.1.1.23: With NAD(+) or NADP(+) as acceptor
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

80-152 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P45353

Entry ID Method Resolution Chain Position Source
AF-P45353-F1 Predicted AlphaFoldDB

No variants for P45353

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P45353

No associated diseases with P45353

2 regional properties for P45353

Type Name Position InterPro Accession
conserved_site Histidinol dehydrogenase, conserved site 638 - 670 IPR001692
domain Phosphoribosyl-AMP cyclohydrolase domain 213 - 284 IPR002496

Functions

Description
EC Number 1.1.1.23 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

6 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
histidinol dehydrogenase activity Catalysis of the reaction: L-histidinol + NAD+ = L-histidine + NADH + H+.
metal ion binding Binding to a metal ion.
NAD binding Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
phosphoribosyl-AMP cyclohydrolase activity Catalysis of the reaction: 1-(5-phosphonatoribosyl)-5'-AMP + H(2)O = 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide.
phosphoribosyl-ATP diphosphatase activity Catalysis of the reaction: 1-(5-phospho-D-ribosyl)-ATP + H(2)O = 1-(5-phosphonatoribosyl)-5'-AMP + diphosphate + H(+).

1 GO annotations of biological process

Name Definition
histidine biosynthetic process The chemical reactions and pathways resulting in the formation of histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTFPLLPAYA SVAEFDNSLS LVGKAVFPYA ADQLHNLIKF TQSTELQVNV QVESSVTEDQ
70 80 90 100 110 120
FEELIDNLLK LYNNGINEVI LDLDLAERVV QRIPGARVIY RTLVDKVASL PANASIAVPF
130 140 150 160 170 180
SSPLGDLKSF TNGGSRTVYA FSETAKLVDV TSTVASGIIP IIDARQLTTE YELSEDVKKF
190 200 210 220 230 240
PVSEILLASL TTDRPDGLFT TLVADSSNYS LGLVYSSKKS IPEAIRTQTG VYQSRRHGLW
250 260 270 280 290 300
YKGATSGATQ KLLGIELDCD GDCLKFVVEQ TGVGFCHLER TSCFGQSKGL RAMEATLWDR
310 320 330 340 350 360
KSNAPEGSYT KRLFDDEVLL NAKIREEADE LAEAKSKEDI AWECADLFYF ALVRCAKYGV
370 380 390 400 410 420
TLDEVERNLD MKSLKVTRRK GDAKPGYTKE QPKEESKPKE VPSEGRIELC KIDVSKASSQ
430 440 450 460 470 480
EIEDALRRPI QKTEQIMELV KPIVDNVRQN GDKALLELTA KFDGVALKTP VLEAPFPEEL
490 500 510 520 530 540
MQLPDNVKRA IDLSIDNVRK FHEAQLAETL QVETCPGVVC SRFARPIEKV GLYIPGGTAI
550 560 570 580 590 600
LPSTSLMLGV PAKVAGCKEI VFASPPKKDG TLTPEVIYVA HKVGAKCIVL AGGAQAVAAM
610 620 630 640 650 660
AYGTETVPKC DKIFGPGNQF VTAAKMMVQN DTSALCSIDM PAGPSEVLVI ADKYADPDFV
670 680 690 700 710 720
VSDLLSQAEH GIDSQVILLA VDMTDKELAR IEDAVHNQAV QLPRVEIVRK CIAHSTTLSV
730 740 750 760 770 780
ATYEQALEMS NQYAPEHLIL QIENASYVDQ VQHAGSVFVG AYSPESCGDY SSGTNHTLPT
790 800 810 820 830 840
YGYARQYSGV NTATFQKFIT SQDVTPEGLK HIGQAVMDLA AVEGLDAHRN AVKVRMEKLG
LI